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    Gel Phase Membrane Retards Amyloid beta-Peptide (1-42) Fibrillation by Restricting Slaved Diffusion of Peptides on Lipid Bilayers

    Year: 2018

    Journal: Langmuir, Volume 34, JUL 17, page 8408–8414

    Authors: Yang, Mengting; Wang, Kang; Lin, Jiake; Wang, Liqun; Wei, Feng; Zhu, Jintao; Zheng, Wanquan; Shen, Lei

    Organizations: National Natural Science Foundation of China [21574051, 21404046]; Excellent Dissertation Cultivation Project of Wuhan University of Technology [2017-YS-080]; Fundamental Research Funds for the Central Universities [WUT: 2018IVA021]

    Plasma membranes in the human brain can interact with amyloid beta-peptide (1-42; A beta(42)) and induce A beta(42) fibrillation, which is considered to be a crucial process underlying the neurotoxicity of A beta(42) and the pathogenesis of Alzheimer's disease (AD). However, the mechanism of membrane-mediated A beta(42) fibrillation at the molecular level remains elusive. Here we study the role of adsorbed A beta(42) peptides on membrane-mediated fibrillation using supported lipid bilayers of varying phase structures (gel and fluid). Using total internal reflection fluorescence microscopy and interfacial specific second-order nonlinear optical spectroscopy, we show that the dynamics of 2D-mobile A beta(42) molecules, facilitated by the highly mobile lipids underneath the peptides, are critical to A beta(42) fibrillation on liquid phase membranes. This growth mechanism is retarded on gel phase membranes where the dynamics of 2D-mobile peptides are restricted by the "frozen" lipids with less mobility.
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