title: 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.
authors.affiliation: Department of Chemistry, State University of New York at Binghamton, Binghamton, New York 13902, United States.
authors.forename: Rumonat D
authors.initials: RD
authors.lastname: Akinlolu
authors.affiliation: Department of Chemistry, State University of New York at Binghamton, Binghamton, New York 13902, United States.
authors.forename: Mimi
authors.initials: M
authors.lastname: Nam
authors.affiliation: Department of Chemistry, State University of New York at Binghamton, Binghamton, New York 13902, United States.
authors.forename: Wei
authors.initials: W
authors.lastname: Qiang
mesh_terms: D016229:Amyloid beta-Peptides / Q000737:chemistry*; D002462:Cell Membrane / Q000737:chemistry*; D006801:Humans; D008081:Liposomes / Q000737:chemistry*; D008561:Membrane Fusion; D008956:Models, Chemical
chemical_list: D016229:Amyloid beta-Peptides; D008081:Liposomes