Insights into the mechanisms of action of host defence peptides from biophysical and structural investigations

被引:73
作者
Bechinger, Burkhard [1 ]
机构
[1] Univ Strasbourg, CNRS, Inst Chim, UMR7177, F-67070 Strasbourg, France
关键词
magainin; alamethicin; solid-state NMR; uniaxially oriented membranes; membrane topology; hydrophobic mismatch; cecropin; in-plane orientation; transmembrane alignment; peptide-lipid interactions; PGLa; peptaibol; membrane pore; membrane macroscopic phase; equlibria; SOLID-STATE NMR; MAGAININ ANTIBIOTIC PEPTIDES; HISTIDINE-RICH PEPTIDES; ANTIMICROBIAL PEPTIDES; ANTIBACTERIAL PEPTIDES; LIPID-BILAYERS; MEMBRANE INSERTION; HELICAL PEPTIDES; CYTOTOXIC AGENTS; ORIENTED N-15;
D O I
10.1002/psc.1343
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
070307 [化学生物学]; 071010 [生物化学与分子生物学];
摘要
In order to better understand the mechanisms of action of linear cationic host defense peptides, biophysical and structural investigations of their interactions with membranes and with other biomacromolecules are reviewed. In particular, an extensive overview will be given of the topological studies of magainins in a number of different lipid environments. Furthermore, amphipathic helices have been designed in such a manner to allow the easy control of their membrane alignment. These peptides not only exhibit potent antimicrobial and transfection activities, but their investigation has also provided important insights into mechanistic aspects of their biological functions. Copyright (C) 2011 European Peptide Society and John Wiley & Sons, Ltd.
引用
收藏
页码:306 / 314
页数:9
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