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

Adree Khondker; Richard J Alsop; Maikel C Rheinstädter

doi:10.3390/membranes7030049

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

Membranes (Basel). 2017 Aug 31;7(3):49. doi: 10.3390/membranes7030049.

Authors

Adree Khondker¹, Richard J Alsop², Maikel C Rheinstädter³

Affiliations

¹ Department of Physics and Astronomy, McMaster University, 1280 Main Street West, Hamilton, ON L8S 4M1, Canada. khondkea@mcmaster.ca.
² Department of Physics and Astronomy, McMaster University, 1280 Main Street West, Hamilton, ON L8S 4M1, Canada. alsoprj@mcmaster.ca.
³ Department of Physics and Astronomy, McMaster University, 1280 Main Street West, Hamilton, ON L8S 4M1, Canada. rheinstadter@mcmaster.ca.

Abstract

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.

Keywords: Alzheimer’s disease; amyloid-β; cross-β sheet; hydrophobic fragment.