Misfolding of amyloidogenic proteins at membrane surfaces:: The impact of macromolecular crowding

被引：62

作者：

Bokvist, Marcus ^{[1
]}

Grobner, Gerhard ^{[1
]}

机构：

[1] Umea Univ, Dept Chem, S-90187 Umea, Sweden

来源：

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 2007年 / 129卷 / 48期

关键词：

D O I：

10.1021/ja076059o

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

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 A beta-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.

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页码：14848 / +

页数：3

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