Despite of effective actions of antimicrobial peptides (AMPs) against antibiotic-resistant bacteria, low antimicrobial activity compared to chemical-based antibiotics has been a limitation for the practical applications. Therefore, there have been various efforts that establish structure-activity relationship (SAR) of AMPs by regulating their structural determinants. In this study, SAR was investigated with KL model AMPs using novel FRET-based AMP activity assay which takes the property of EGFP mutants, differential stabilities based on pH. The design of KL model AMPs was focused on the examination for distribution effect of cationic amino acids on the hydrophilic surface of helical wheel. All of KL analogues having a-helical structures followed a hypothesis that antimicrobial activity of AMPs is enhanced as cationic amino acids are uniformly distributed on the hydrophilic surface. This hypothesis was confirmed with natural AMP, CRAMP18, and its analogues, which had a-helical structures. CRAMP18 analogues showed improved antimicrobial activity from the accumulation of lysine switches which made uniform distribution of positive amino acids. Therefore, we suggest that antimicrobial activities of AMPs can be improved by rearranging cationic amino acids to have high dispersity based on helical wheel structure.
키워드
Antimicrobial peptidefluorescence resonance energy transferstructure-activity relationshipalpha-helixpH
저자
Young Soo KIM [ Dept. of Chemical Engineering, POSTECH, Pohang, 790-784. ]
Hyung Joon CHA [ Dept. of Chemical Engineering, POSTECH, Pohang, 790-784. ]
한국생물공학회 [The Korean Society for Biotechnology and Bioengineering]
설립연도
1984
분야
공학>생물공학
소개
이 법인은 생물 공학의 발전과 보급에 이바지하고, 회원 상호 간의 연구 협력과 친목을 도모함을 목적으로 한다
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