The relationship between peptide structure and antibacterial activity

被引:804
作者
Powers, JPS [1 ]
Hancock, REW [1 ]
机构
[1] Univ British Columbia, Dept Microbiol & Immunol, Vancouver, BC V6T 1Z3, Canada
基金
加拿大自然科学与工程研究理事会;
关键词
antimicrobial cationic peptide; polyphemusin; structure;
D O I
10.1016/j.peptides.2003.08.023
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Cationic antimicrobial peptides are a class of small, positively charged peptides known for their broad-spectrum antimicrobial activity. These peptides have also been shown to possess anti-viral and anti-cancer activity and, most recently, the ability to modulate the innate immune response. To date, a large number of antimicrobial peptides have been chemically characterized, however, few high-resolution structures are available. Structure-activity studies of these peptides reveal two main requirements for antimicrobial activity, (1) a cationic charge and (2) an induced amphipathic conformation. In addition to peptide conformation, the role of membrane lipid composition, specifically non-bilayer lipids, on peptide activity will also be discussed. (C) 2003 Elsevier Inc. All rights reserved.
引用
收藏
页码:1681 / 1691
页数:11
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