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α-螺旋肽的膜结合和孔形成。

Membrane association and pore formation by alpha-helical peptides.

机构信息

lnstitut de chimie, CNRS-Université de Strasbourg, UMR 7177, 4, rue Blaise Pascal, 67070 Strasbourg, France.

出版信息

Adv Exp Med Biol. 2010;677:24-30. doi: 10.1007/978-1-4419-6327-7_3.

Abstract

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.

摘要

膜活性肽具有抗菌、形成通道和运输活性,因此很早就成为生物物理研究的有趣目标。当研究肽-脂相互作用时,会出现一种动态观点,即肽在插入膜时会改变构象,可以采用多种拓扑结构,并局部或全局改变膜的宏观相性质。有趣的是,已经鉴定出几种以动态方式与膜相互作用的蛋白质,并且从肽中学到的经验可能有助于我们理解这些蛋白质的功能方式。

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