Amyloidogenic Protein Membrane Interactions: Mechanistic Insight from Model Systems

被引：491

作者：

Butterfield, Sara M. ^{[1
]}

Lashuel, Hilal A. ^{[1
]}

机构：

[1] Ecole Polytech Fed Lausanne, Swiss Fed Inst Technol Lausanne, Lab Mol Neurobiol & Neuroprote, CH-1015 Lausanne, Switzerland

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2010年 / 49卷 / 33期

基金：

瑞士国家科学基金会;

关键词：

amyloid toxicity; artificial membranes; fibrillogenesis; permeabilization; pore-forming proteins; SOLID-STATE NMR; SUPPORTED LIPID-BILAYERS; BOUND ALPHA-SYNUCLEIN; PORE-FORMING PEPTIDES; BETA ION CHANNELS; C-TERMINAL DOMAIN; ALZHEIMERS-DISEASE; ANTIMICROBIAL PEPTIDES; PARKINSONS-DISEASE; A-BETA;

D O I：

10.1002/anie.200906670

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

The toxicity of amyloid-forming proteins is correlated with their interactions with cell membranes. Binding events between amyloidogenic proteins and membranes result in mutally disruptive structural perturbations, which are associated with toxicity. Membrane surfaces promote the conversion of amyloid-forming proteins into toxic aggregates, and amyloidogenic proteins, in turn, compromise the structural integrity of the cell membrane. Recent studies with artificial model membranes have highlighted the striking resemblance of the mechanisms of membrane permeabilization of amyloid-forming proteins to those of pore-forming toxins and antimicrobial peptides. © 2010 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.

引用

页码：5628 / 5654

页数：27

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