Fibrillization of β-Amyloid Peptides via Chemically Modulated Pathway

Abstract

The aggregation of β-amyloid peptides is closely associated with Alzheimer's disease. We have used liposomes to modulate the early aggregation events of 40-residue β-amyloid peptides. The spatial confinement provided by liposomes leads to the formation of nonfibrillar aggregates of β-amyloid peptides. These on-pathway β-sheet intermediates were used to seed the fibrillization of the monomer peptides. Solid-state NMR spectroscopy revealed that the resultant fibrils have a more uniform structure than those formed in liposome-free solution.

Keywords: Alzheimer's disease; nucleation; peptides; peptidic fibrils; polymorphism; seeding effects.