Document Type
Article
Publication Date
Fall 2011
Abstract
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.
Volume
6
Issue
6
First Page
20575
Recommended Citation
Zheng, Jie, "Polymorphic Structures of Alzheimer's Beta-amyloid Globulomers" (2011). Chemical, Biomolecular, and Corrosion Engineering Faculty Research. 273.
https://ideaexchange.uakron.edu/chemengin_ideas/273