Membrane Association and Pore Formation by Alpha-Helical Peptides

被引:0
|
作者
Bechinger, Burkhard [1 ]
机构
[1] Univ Strasbourg, CNRS, UMR 7177, Inst Chim, F-67070 Strasbourg, France
关键词
SOLID-STATE NMR; SURFACE-PLASMON RESONANCE; PROTEIN DATA-BANK; ANTIMICROBIAL PEPTIDES; ION CHANNELS; LIPID-BILAYERS; PHOSPHOLIPID-BILAYERS; MAGAININ PEPTIDES; FORMING COLICINS; PROTON CHANNEL;
D O I
暂无
中图分类号
R-3 [医学研究方法]; R3 [基础医学];
学科分类号
1001 ;
摘要
Membrane-active peptides exhibit antimicrobial, channel-forming and transport activities and have therefore early on been interesting targets for biophysical investigations. When the peptide-lipid interactions are studied a dynamic view emerges in which the peptides change conformation upon membrane insertion, can adopt a variety of topologies and change the macroscopic phase properties of the membrane locally or globally. Interestingly several proteins have been identified that also interact with the membrane in a dynamic fashion and where the lessons learned from peptides may add to our understanding of the ways these proteins function.
引用
收藏
页码:24 / 30
页数:7
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