Amphiphilic α-helical antimicrobial peptides and their structure/function relationships

被引：157
|
作者：
Dennison, SR
Wallace, J
Harris, F
Phoenix, DA [1 ]
机构：
[1] Univ Cent Lancashire, Fac Sci, Deans Off, Preston PR1 2HE, Lancs, England
[2] Univ Cent Lancashire, Dept Forens & Investigat Sci, Preston PR1 2HE, Lancs, England
[3] Univ Cent Lancashire, Dept Phys Math & Astron, Preston PR1 2HE, Lancs, England
来源：
PROTEIN AND PEPTIDE LETTERS | 2005年 / 12卷 / 01期
关键词：
D O I：
10.2174/0929866053406084
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：
To facilitate microbial membrane invasion, amphiphilic alpha-helical antimicrobial peptides (alpha-AMPs) show a spatial segregation of hydrophobic and hydrophilic residues about the alpha-helical long axis. Here we discuss potential mechanisms by which these peptides are able to disrupt membrane structure and the structural characteristics, which are required for function.
引用
收藏
页码：31 / 39
页数：9
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