Describing the Mechanism of Antimicrobial Peptide Action with the Interfacial Activity Model

被引:792
作者
Wimley, William C. [1 ]
机构
[1] Tulane Univ, Hlth Sci Ctr, Dept Biochem SL43, New Orleans, LA 70112 USA
基金
美国国家卫生研究院;
关键词
RATIONAL COMBINATORIAL DESIGN; CELL-PENETRATING PEPTIDES; OR-NONE PERMEABILIZATION; AMPHIPATHIC BETA-SHEET; PORE FORMATION; MAGAININ; QUANTITATIVE MODEL; LIPID-MEMBRANES; DELTA-LYSIN; X-RAY;
D O I
10.1021/cb1001558
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
Antimicrobial peptides (AMPs) have been studied for three decades, and yet a molecular understanding of their mechanism of action is still lacking. Here we summarize current knowledge fro both synthetic vesicle experiments and microbe experiments, with a focus on comparisons between the two. Microbial experiments are done at peptide to lipid ratios that are at least 4 orders of magnitude higher than vesicle-based experiments. To close the gap between the two concentration regimes, we propose an "interfacial activity model", which is based on an experimentally testable molecular image of AMP-membrane interactions. The interfacial activity model may be useful in driving engineering and design of novel AMPs.
引用
收藏
页码:905 / 917
页数:13
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