The Polymorphic Nature of Membrane-Active Peptides from Biophysical and Structural Investigations

被引:22
作者
Bechinger, Burkhard [1 ]
Aisenbrey, Christopher [1 ]
机构
[1] Univ Strasbourg, CNRS, UMR7177, Inst Chim,Fac Chim, F-67070 Strasbourg, France
关键词
Alamethicin; cecropin; hydrophobic mismatch; membrane topology; solid-state NMR; supported bilayers; SOLID-STATE NMR; CELL-PENETRATING PEPTIDES; HISTIDINE-RICH PEPTIDES; NUCLEAR-MAGNETIC-RESONANCE; SODIUM DODECYL-SULFATE; MAGAININ; AMIDE; ANTIMICROBIAL PEPTIDES; LIPID-BILAYERS; ANTIBACTERIAL PEPTIDES; ANTIBIOTIC PEPTIDES;
D O I
10.2174/138920312804142093
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
Membrane-active peptides exhibit a wide variety of biological functions including pore formation, signaling and antimicrobial activities. They are also capable of transporting large cargo such as proteins or nucleic acids across cell membranes. This review summarizes biophysical and structural investigations on hydrophobic, amphipathic and heavily charged peptides that reveal a very dynamic view on their membrane interactions. Individual peptides are able to adopt a variety of different conformations and topology and at the same time exhibit multimodal functionalities. Examples discussed in this paper include peptaibols, magainins, cell penetrating peptides and designed histidine-rich sequences with potent antimicrobial and nucleic acid transfection activities.
引用
收藏
页码:602 / 610
页数:9
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