Effect of the surface charge of artificial model membranes on the aggregation of amyloid 尾-peptide

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• 作者：Raimon Sabaté ; ^a ; ^b ; ^{raimon.sabate@uab.cat} ; Alba Espargaró ; ^a ; Lucyanna Barbosa-Barros^b ; Salvador Ventura^a ; Joan Estelrich^b ; ^c ; ^{joanestelrich@ub.edu}
• 关键词：Amyloid ; Oligomer ; Fibrils ; Liposome ; Aggregation ; Model membrane
• 刊名：Biochimie
• 出版年：2012
• 期刊代码：24_03009084
• 类别：bio
• 出版时间：August, 2012
• 卷：94
• 期：8
• 页码：1730-1738
• 文件大小：1121 K

摘要

The neurotoxicity effect of the 尾-amyloid (A尾) peptide, the primary constituent of senile plaques in Alzheimer's disease, occurs through interactions with neuronal membranes. Here, we attempt to clarify the mechanisms and consequences of the interaction of A尾 with lipid membranes. We have used liposomes as a model of biological membrane, and have devoted particular attention to the bilayer charge effect. Our results show that insertion and surface association of peptide with membrane, increased in a membrane charge-dependent manner, lead to a reduction of A尾 soluble species, lag time elongation and an increase in the inter-molecular 尾-sheet ratio of amyloid fibrils. In addition, our findings suggest that the fine balance between peptide insertion and surface association modulates A尾 aggregation, influencing the amyloid fibrils concentration as well as their morphology.