Abstract

Alzheimer's disease is a progressive, neurodegenerative disorder characterized by amyloid deposition in senile plaques in the cerebral parenchyma and vasculature.(1) These plaques are composed primarily of fibers of the amyloid β-protein, Aβ. A number of studies have provided information on the structure of fibrils formed both in vivo and in vitro, and on factors affecting fiber formation. Synthetic Aβ peptides also form fibers which are ultrastructurally indistinguishable from those isolated from the brain. These peptides have been utilized to examine how a variety of parameters, including temperature, pH, solvent composition, peptide concentration, and peptide sequence, influence the final structure of Aβ aggregates. What is substantially less understood, however, is the kinetics of Aβ fibril growth.

© 1996 Optical Society of America