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
Biochemistryjournal_title
Biochemistryauthors
Akinlolu RD,Nam M,Qiang Wdoi
10.1021/acs.biochem.5b00321subject
Has Abstractpub_date
2015-06-09 00:00:00pages
3416-9issue
22eissn
0006-2960issn
1520-4995journal_volume
54pub_type
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