Competition between Fibrillation and Induction of Vesicle Fusion for the Membrane-Associated 40-Residue β-Amyloid Peptides
Competition between Fibrillation and Induction of Vesicle Fusion for the Membrane-Associated 40-Residue β-Amyloid Peptides
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DOI：
10.1021/acs.biochem.5b00321
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发表时间：
2015-06-09
期刊：
影响因子：
2.9
通讯作者：
Qiang, Wei
中科院分区：
文献类型：
--
作者：
Akinlolu, Rumonat D.;Nam, Mimi;Qiang, Wei
β -淀粉样蛋白（A β）肽破坏细胞膜被认为是阿尔茨海默病的主要机制。多肽与脂质摩尔比（P:L）在一个广泛的生物范围内变化。我们在此报告，当模型A β脂质体系统中P:L变化时，先前观察到的两种A β进化途径，纤颤和诱导囊泡融合，相互竞争。高P:L时更倾向于纤颤，低P:L时促进融合。结构研究表明，A β中相同的残基可能参与融合位点的初始纤颤和膜结合。
Disruption of the cell membrane by the beta-amyloid (A beta) peptides has been considered as a main mechanism of Alzheimer's disease. The peptide-to-lipid molar ratio (P:L) varies over a broad lunge biologically. We report here that two of the previously observed A beta evolution pathways, fibrillation and induction of vesicle fusion, compete with each other when P:L varies in model A beta-liposome systems. Fibrillation is preferred at higher P:L values, and fusion is promoted at lower P:L values. Structural studies suggest that the same residues in A beta may involve in both the initial fibrillation and membrane binding at the fusion sites.