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双层膜中短杆菌肽A'-磷脂相互作用的模型。

A model for gramicidin A'-phospholipid interactions in bilayers.

作者信息

Cornell B A, Separovic F

机构信息

CSIRO Division of Food Processing, North Ryde, NSW, Australia.

出版信息

Eur Biophys J. 1988;16(5):299-306. doi: 10.1007/BF00254066.

Abstract

A model is proposed for the effect of gramicidin A' on the order and structure of phospholipid dispersions. According to this model, the addition of gramicidin A' influences the surrounding lipids via two independent mechanisms. The first arises from a drop in surface pressure for those lipids substantially bounded by gramicidin A'. The second mechanism arises from the increase in the phospholipid headgroup spacing due to the small polar region of the polypeptide. The model provides an explanation for the currently available NMR, X-ray diffraction and Langmuir monolayer results. The model also suggests mechanisms for the ability of gramicidin A' to trigger a transition of the lipid from the lamellar to hexagonal II phase, the dependence of this transition on the lipid chain length and the formation of a lamellar phase with lysophosphatidylcholine.

摘要

提出了一个关于短杆菌肽A'对磷脂分散体的有序性和结构影响的模型。根据该模型,短杆菌肽A'的添加通过两种独立机制影响周围的脂质。第一种机制源于那些被短杆菌肽A'大量包围的脂质表面压力的下降。第二种机制源于多肽的小极性区域导致的磷脂头部基团间距增加。该模型为目前可用的核磁共振、X射线衍射和朗缪尔单层结果提供了解释。该模型还提出了短杆菌肽A'触发脂质从层状相转变为六方II相的能力、这种转变对脂质链长度的依赖性以及与溶血磷脂酰胆碱形成层状相的机制。

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