Competition between Fibrillation and Induction of Vesicle Fusion for the Membrane-Associated 40-Residue β-Amyloid Peptides.

Abstract:

:Disruption of the cell membrane by the β-amyloid (Aβ) peptides has been considered as a main mechanism of Alzheimer's disease. The peptide-to-lipid molar ratio (P:L) varies over a broad range biologically. We report here that two of the previously observed Aβ evolution pathways, fibrillation and induction of vesicle fusion, compete with each other when P:L varies in model Aβ-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 Aβ may involve in both the initial fibrillation and membrane binding at the fusion sites.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Akinlolu RD,Nam M,Qiang W

doi

10.1021/acs.biochem.5b00321

subject

Has Abstract

pub_date

2015-06-09 00:00:00

pages

3416-9

issue

22

eissn

0006-2960

issn

1520-4995

journal_volume

54

pub_type

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