期刊
FEBS LETTERS
卷 583, 期 14, 页码 2425-2428出版社
WILEY
DOI: 10.1016/j.febslet.2009.06.044
关键词
Antimicrobial peptide; Cytolytic peptide; Hemolytic activity; Molecular modeling; Molecular hydrophobicity potential; Protein engineering
资金
- Russian Foundation for Basic Research [07-0401166, 08-04-00454, 07-04-01514]
- Russian Federation Federal Agency for Science and Innovations [SS-4728.2006.4, MK-69.2008.4]
- RAS Programmes
In silico structural analyses of sets of alpha-helical antimicrobial peptides (AMPs) are performed. Differences between hemolytic and non-hemolytic AMPs are revealed in organization of their N-terminal region. A parameter related to hydrophobicity of the N-terminal part is proposed as a measure of the peptide propensity to exhibit hemolytic and other unwanted cytotoxic activities. Based on the information acquired, a rational approach for selective removal of these properties in AMPs is suggested. A proof of concept is gained through engineering specific mutations that resulted in elimination of the hemolytic activity of AMPs (latarcins) while leaving the beneficial antimicrobial effect intact. (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据