期刊
JOURNAL OF PEPTIDE SCIENCE
卷 19, 期 12, 页码 792-800出版社
WILEY
DOI: 10.1002/psc.2578
关键词
antibacterial peptides; Gram-positive bacteria; cationic homopeptides; polyproline II helix; Arg; Lys
资金
- FONDECYT - Chile Grant [1100556]
In the selection or design of antimicrobial peptides, the key role played by cationic amino acids and chain length on the inhibitory potency and specificity is not clear. A fundamental study was conducted using chemically synthesized homopeptides of l-Lys and l-Arg ranging from 7 to 14 residues. Their effect on growth inhibition was evaluated over a wide range of Gram-positive bacteria at different levels of concentration. Interestingly, at lower concentrations (10M), Lys homopeptides with odd number of residues, especially with 11 residues, showed a broader inhibitory activity than those with even number of residues. At higher peptide concentrations (>20M), the inhibitory activity of Lys homopeptides was directly related to the number of residues in the chain. In contrast, Arg homopeptides, at lower concentrations, did not exhibit a defined pattern of bacterial inhibition related to the number of residues; however, at higher concentrations (>20M), the inhibitory effects were more pronounced. Lys homopeptides at concentrations up to 300M showed a remarkably lower toxicity against CHSE-214 cells. Arg homopeptides exhibited negligible cytotoxicity up to chain length of 11 residues at concentrations lower than 100M, but an abrupt increase in toxicity resulted when the peptide chain length reached 12 amino acid residues and higher concentrations. All synthesized homopeptides displayed characteristic polyproline II helix conformation in both buffer and liposomes, as shown by CD spectroscopy. This result suggests that short Lys homopeptides with an odd number of residues (9 and 11) have a broad spectrum of activity against Gram-positive bacterial cells compared with Arg homopeptides, which in turn showed a considerably higher selectivity toward those cells. By investigating the differences between Lys and Arg homopeptides, this study contributes to the understanding of their mechanism of growth inhibition and selectivity. Thus, it provides further guidelines for a rational design of short antimicrobial peptides. Copyright (c) 2013 European Peptide Society and John Wiley & Sons, Ltd.
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