Polymorphic structures of Alzheimer's β-amyloid globulomers.

ABSTRACT:

Background

Misfolding and self-assembly of Amyloid-β (Aβ) peptides into amyloid fibrils is pathologically linked to the development of Alzheimer's disease. Polymorphic Aβ structures derived from monomers to intermediate oligomers, protofilaments, and mature fibrils have been often observed in solution. Some aggregates are on-pathway species to amyloid fibrils, while the others are off-pathway species that do not evolve into amyloid fibrils. Both on-pathway and off-pathway species could be biologically relevant species. But, the lack of atomic-level structural information for these Aβ species leads to the difficulty in the understanding of their biological roles in amyloid toxicity and amyloid formation.

Methods and findings

Here, we model a series of molecular structures of

SUBMITTER: Yu X 

PROVIDER: S-EPMC3110195 | biostudies-literature | 2011

REPOSITORIES: biostudies-literature