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膜表面淀粉样蛋白的错误折叠:大分子拥挤效应的影响

Misfolding of amyloidogenic proteins at membrane surfaces: the impact of macromolecular crowding.

作者信息

Bokvist Marcus, Gröbner Gerhard

机构信息

Department of Chemistry, University of Umeå, 90187 Umeå, Sweden.

出版信息

J Am Chem Soc. 2007 Dec 5;129(48):14848-9. doi: 10.1021/ja076059o. Epub 2007 Nov 9.

DOI:10.1021/ja076059o
PMID:17990885
Abstract

The presence of inert macromolecular crowding agents mimics the situation in vivo where amyloidogenic proteins are released into an aqueous, congested intracellular environment. By using the amphiphatic Alzheimer Abeta-protein as the model system, the presence of a three-dimensional macromolecular crowding environment enhanced significantly its misfolding behavior if charged membrane surfaces as two-dimensional aggregation templates were present.

摘要

惰性大分子拥挤剂的存在模拟了体内的情况,即淀粉样蛋白被释放到一个水相的、拥挤的细胞内环境中。以两亲性的阿尔茨海默病β-蛋白作为模型系统,如果存在作为二维聚集模板的带电膜表面,三维大分子拥挤环境的存在会显著增强其错误折叠行为。

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