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

被引：158

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.

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收藏

页码：31 / 39

页数：9

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