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Membranes 2017, 7(3), 49;

Membrane-Accelerated Amyloid-β Aggregation and Formation of Cross-β Sheets

Department of Physics and Astronomy, McMaster University, 1280 Main Street West, Hamilton, ON L8S 4M1, Canada
Author to whom correspondence should be addressed.
Received: 12 June 2017 / Revised: 26 July 2017 / Accepted: 23 August 2017 / Published: 31 August 2017
(This article belongs to the Special Issue Biological, Biomimetic, and Biomedical Applications of Membranes)
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Amyloid- β aggregates play a causative role in Alzheimer’s disease. These aggregates are a product of the physical environment provided by the basic neuronal membrane, composed of a lipid bilayer. The intrinsic properties of the lipid bilayer allow amyloid- β peptides to nucleate and form well-ordered cross- β sheets within the membrane. Here, we correlate the aggregation of the hydrophobic fragment of the amyloid- β protein, A β 25 - 35 , with the hydrophobicity, fluidity, and charge density of a lipid bilayer. We summarize recent biophysical studies of model membranes and relate these to the process of aggregation in physiological systems. View Full-Text
Keywords: Alzheimer’s disease; amyloid-β; hydrophobic fragment; cross-β sheet Alzheimer’s disease; amyloid-β; hydrophobic fragment; cross-β sheet

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Khondker, A.; Alsop, R.J.; Rheinstädter, M.C. Membrane-Accelerated Amyloid-β Aggregation and Formation of Cross-β Sheets. Membranes 2017, 7, 49.

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