• • DRAMP ID

  • DRAMP03186

• • Peptide Name

  • Spheniscin-2 (Sphe-2; penguin avian beta-defensin 103b; birds ,animals)

• • Source

  • Aptenodytes patagonicus (King penguin)

• • Family

  • Belongs to the beta-defensin family

• • Gene

  • Not found

• • Sequence

  • SFGLCRLRRGFCARGRCRFPSIPIGRCSRFVQCCRRVW

• • Sequence Length

  • 38

• • UniProt Entry

  • P83430

• • Protein Existence

  • Protein level

• • Biological Activity

  • Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal

• • Target Organism

  • • [Ref.14525994]Gram-positive bacteria: Micrococcus luteus (MIC=1.5-3.0 µM), Bacillus subtilis (MIC=0.8-1.5 µM), Bacillus cereus ATCC 11778 (MIC=3-6 µM), Bacillus megaterium (MIC=0.4-0.8 µM), Staphylococcus aureus (MIC=1.5-3.0 µM), Staphylococcus saprophyticus (MIC=1.5-3.0 µM), Staphylococcus haemolyticus (MIC=1.5-3.0 µM), Nocardia asteroides (MIC=0.8-1.5 µM), Aerococcus viridans (MIC=0.4-0.8 µM), Listeria monocytogenes (MIC=6-12 µM);
    • Gram-negative bacteria: Escherichia coli SBS 363 (MIC=0.8-1.5 µM), Escherichia coli 1106 (MIC=1.5-3.0 µM), Salmonella typhimurium (MIC=6-12 µM), Klebsiella pneumoniae (MIC=50-100 µM), Pseudomonas aeruginosa ATCC 82118 (MIC=6-12 µM), Vibrio metschnikovii NCTC 8483 (MIC=25-50 µM), Vibrio anguillarum ATCC 19264 (MIC=25-50 µM);
    • Fungi: Candida glabrata (MIC>100 µM), Candida albicans IHEM 8060 (MIC=50-100 µM), Candida tropicalis (MIC=1.5-3.0 µM), Neurospora crassa (MIC=3-6 µM),Aspergillus fumigatus (MIC=3-6 µM).

• • Hemolytic Activity

  • • It has hemolytic activity

• • Cytotoxicity

  • No cytotoxicity information found in the reference(s) presented

• • Binding Target

  • Not found

• • Linear/Cyclic

  • Cyclic

• • N-terminal Modification

  • Free

• • C-terminal Modification

  • Free

• • Nonterminal Modifications and Unusual Amino Acids

  • Disulfide bonds between Cys5 and Cys33; Cys12 and Cys27; Cys17 and Cys34.

• • Stereochemistry

  • L

• • Structure

  • Beta strand (3 strands; 14 residues)

• • Structure Description

  • The overall fold of Sphe-2 includes a three-stranded antiparallel beta-sheet stabilized by three disulfide bridges with a pairing typical of beta-defensins. In addition, the N-terminal segment shows helical features on most structures.(Ref.2)

• • Helical Wheel Diagram

  • 

• • PDB ID

  • 1UT3 resolved by NMR.

• Predicted Structure

• There is no predicted structure for DRAMP03186.

DRAMP03186

• • Function

  • Has antimicrobial activity. Has insecticidal and hemolytic activities. Probably acts by disturbing membrane Function

• • PTM

  • Contains three disulfide bond

• • Preserving food in the bird somach for several weeks during egg incubation. The disulfide bond pattern is identical to canonical beta-defensins from mammals. The high potency is related to its high cationicity as well as a hydrophobic patch, which is not observed in mammalian defensins.

• ·Literature 1

• • Title

  • Spheniscins, avian beta-defensins in preserved stomach contents of the king penguin, Aptenodytes patagonicus.

• • Pubmed ID

  • 14525994

• • Reference

  • J Biol Chem. 2003 Dec 19;278(51):51053-51058.

• • Author

  • Thouzeau C, Le Maho Y, Froget G, Sabatier L, Le Bohec C, Hoffmann JA, Bulet P.

• ·Literature 2

• • Title

  • Solution structure of spheniscin, a beta-defensin from the penguin stomach.

• • Pubmed ID

  • 15123713

• • Reference

  • J Biol Chem. 2004 Jul 16;279(29):30433-30439.

• • Author

  • Landon C, Thouzeau C, Labbé H, Bulet P, Vovelle F.