Effect of the surface charge of artificial model membranes on the aggregation of amyloid ¦Â-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
• 出版时间：August, 2012
• 年：2012
• 卷：94
• 期：8
• 页码：1730-1738
• 全文大小：1121 K

文摘

The neurotoxicity effect of the ¦Â-amyloid (A¦Â) 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¦Â 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¦Â soluble species, lag time elongation and an increase in the inter-molecular ¦Â-sheet ratio of amyloid fibrils. In addition, our findings suggest that the fine balance between peptide insertion and surface association modulates A¦Â aggregation, influencing the amyloid fibrils concentration as well as their morphology.