De novo generation of antimicrobial LK peptides with a single tryptophan at the critical amphipathic interface

De novo design of amphipathic model peptides has been successful for generating many antimicrobial peptides with various lengths and amino acid compositions. Here, we suggest a very simple strategy to design antimicrobial peptides with a short length and a simple amino acid composition. Amphipathic...

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Bibliographic Details
Published in:Journal of peptide science 2009-09, Vol.15 (9), p.583-588
Main Authors: Kang, Su-Jin, Won, Hyung-Sik, Choi, Wahn-Soo, Lee, Bong-Jin
Format: Article
Language:English
Subjects:
Amino Acid Sequence
amphipathic helix
Antimicrobial Cationic Peptides - chemical synthesis
Antimicrobial Cationic Peptides - chemistry
Antimicrobial Cationic Peptides - pharmacology
antimicrobial peptides
Circular Dichroism
critical amphipathic interface
de novo design
Gram-Negative Bacteria - drug effects
Gram-Positive Bacteria - drug effects
Hemolysis - drug effects
Humans
LK peptides
Microbial Sensitivity Tests
Molecular Sequence Data
Structure-Activity Relationship
tryptophan
Tryptophan - chemistry
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Summary:De novo design of amphipathic model peptides has been successful for generating many antimicrobial peptides with various lengths and amino acid compositions. Here, we suggest a very simple strategy to design antimicrobial peptides with a short length and a simple amino acid composition. Amphipathic helical properties were conferred by using only leucines and lysines and a single tryptophan was positioned at the critical amphipathic interface between the hydrophilic ending side and the hydrophobic starting side, in the helical wheel projection. According to this rule, the model peptides with 7 to 13 residues exhibited antimicrobial activity. Among them, the most potent activity against both Gram‐positive and Gram‐negative bacteria, covering all of the nine bacterial strains tested in this study, was found for the 11‐mer sequences having a 1:1 (L5K5W6) or a 3:2 (L6K4W6) ratio of leucines to lysines. In particular, the former peptide L5K5W6 could be evaluated as the most useful agent, as it showed no significant hemolytic activity with a broad‐spectrum of antimicrobial activity. Copyright © 2009 European Peptide Society and John Wiley & Sons, Ltd.
ISSN:1075-2617
1099-1387
DOI:10.1002/psc.1149