Antimicrobial peptides (AMPs) play an important role to cope with invasion of microorganisms. Based on the antimicrobial mechanism of AMPs, there have been considerable efforts to improve the antimicrobial activities of a-helical AMPs in association with structure-activity relationship (SAR) study. In this study, to demonstrate the relationship of distribution of cationic amino acids and antimicrobial activity of AMP, we designed pertinent KL (lysine and leucine) model AMPs to have same hydrophobic arc, net charge, and overall hydrophobicity and investigated effect of cationic amino acid distribution. Next, we confirmed it using natural AMP analogue, CRAMP18, and its derivatives. In results, we observed enhancement of AMP activity by modulation of dispersity for cationic distribution. Thus, we proposed that distribution of cationic amino acids on the hydrophilic surface of helical wheel structure is a determining factor for antimicrobial activity of AMP. It is expected that antimicrobial activities of natural AMPs can be improved by rational redesign of amino acid sequences through rearrangement of positively-charged amino acids on the hydrophilic surface region of helical wheel to have more uniform dispersity as well as parallel regulations of other known structural parameters.
한국생물공학회 [The Korean Society for Biotechnology and Bioengineering]
설립연도
1984
분야
공학>생물공학
소개
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