Membrane-accelerated Amyloid-β aggregation and formation of cross-β sheets

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, Aβ25-35, 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.