General Information
Activity Information
-
Biological Activity
- Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal
-
Target Organism
-
- Gram-negative bacteria: Escherichia coli ATCC25922 (MIC=1 µg/ml), E. coli ML35 (MIC=1 µg/ml), E. coli D21 (MIC=0.25 µg/ml), Salmonella typhimurium ATCC 14028 (MIC=1 µg/ml), Pseudomonas aeruginosa ATCC 27853 (MIC=1 µg/ml), Serratia marcescens ATCC 8100 (MIC=2 µg/ml);
- Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=2 µg/ml), Staphylococcus aureus Cowan 1 (MIC=2 µg/ml), Staphylococcus aureus (MRSA) (MIC=4 µg/ml), S. epidermidis ATCC 12228 (MIC=1 µg/ml), Bacillus megaterium Bm11 (MIC=2 µg/ml).
- Fungi: Candida albicans (MIC=8 µg/ml), Cryptococcus neoformans (MIC=4 µg/ml).
-
Hemolytic Activity
-
- No hemolysis information or data found in the reference(s) presented in this entry
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Cytotoxicity
-
- Not included yet
-
Binding Target
- Not found
Structure Information
-
Linear/Cyclic
- Not included yet
-
N-terminal Modification
- Not included yet
-
C-terminal Modification
- Not included yet
-
Nonterminal Modifications and Unusual Amino Acids
- Not included yet
-
Stereochemistry
- Not included yet
-
Structure
- Alpha helix (2 helices; 19 residues)
-
Structure Description
- Not found
-
Helical Wheel Diagram
-
PDB ID
- 2KET resolved by NMR.
- 2KET-> 
-
Predicted Structure
- Please click DRAMP02855_predicted_structure.pdb to download.
Physicochemical Information
-
Formula
- C160H265N45O29
Absent Amino Acids
- ACDEMNQTWY
Common Amino Acids
- K
Mass
- 3283.15
PI
- 12.32
Basic Residues
- 11
Acidic Residues
- 0
Hydrophobic Residues
- 11
Net Charge
- +11
-
Boman Index
- -44.31
Hydrophobicity
- -0.367
Aliphatic Index
- 97.41
Half Life
-
- Mammalian:30 hour
- Yeast:>20 hour
- E.coli:>10 hour
Extinction Coefficient Cystines
- 0
Absorbance 280nm
- 0
Polar Residues
- 3
DRAMP02855
Comments Information
Function
- Exerts a potent antimicrobial activity against Gram-negative and Gram-positive bacteria, including methicillin-resistant Staphylococcus aureus, and fungi.
PTM
- Contains two disulfide bonds. (By similarity)
Literature Information
- ·Literature 1
-
Title
- Biological characterization of two novel cathelicidin-derived peptides and identification of structural requirements for their antimicrobial and cell lytic activities.
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Pubmed ID
- 8910461
-
Reference
- J. Biol. Chem. 1996;271:28375-28381.
-
Author
- Skerlavaj B, Gennaro R, Bagella L, Merluzzi L, Risso A, Zanetti M.
- ·Literature 2
-
Title
- Sequence analysis and polymorphism discovery in 4 members of the bovine cathelicidin gene family.
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Pubmed ID
- 19136450
-
Reference
- J. Hered. 2009;100:241-245.
-
Author
- Gillenwaters EN, Seabury CM, Elliott JS, Womack JE.
- ·Literature 3
-
Title
- solution structure of BMAP-27.
-
Pubmed ID
- PubMed ID is not available
-
Reference
- To be Published
-
Author
- Yang S, Jung H, Kim J.