Abstract
Conversion of non–toxic soluble amyloid –β protein (Aβ) into cytotoxic aggregates such as oligomers and amyloid fibrils is a critical step in the development of Alzheimer’s disease. A growing body of evidence is accumulating to show that biological membrane vesicles, both inside and outside cells, are involved in multiple processes, including Aβ production, metabolism, aggregation, transport, and clearance. Here, we review the biological studies on the interaction between Aβ and membrane vesicles such as endosomes, multivesicular bodies (MVBs), and exosomes in the pathological brains, animal models, and cultured cells. Subsequently, biochemical and physicochemical studies on the Aβ– lipid interactions that underlie molecular mechanisms of Aβ– vesicle association will be discussed. In addition, a study focusing on the high membrane curvature of intraluminal vesicles of MVBs and exosomes due to their small particle size will be presented. We show that high membrane curvature promotes Aβ binding, structural changes, and fibrillation on lipid bilayer surfaces.
