Evidence of fibril-like β-sheet structures in a neurotoxic amyloid intermediate of Alzheimer's β-amyloid

• Published in: Nature structural & molecular biology Vol. 14; no. 12; pp. 1157 - 1164
• Main Authors: Chimon, Sandra, Shaibat, Medhat A, Jones, Christopher R, Calero, Diana C, Aizezi, Buzulagu, Ishii, Yoshitaka
• Format: Journal Article
• Language: English
• Published: New York Nature Publishing Group US 01.12.2007; Nature Publishing Group
• Subjects: Alzheimer's disease; Amyloid - chemistry; Amyloid beta-Peptides - chemistry; Amyloid beta-Peptides - toxicity; Amyloid beta-Peptides - ultrastructure; Amyloid beta-protein; Animals; Biochemistry; Biological Microscopy; Biomedical and Life Sciences; Care and treatment; Fluorescent Dyes; Genetic aspects; Humans; Life Sciences; Membrane Biology; Microscopy, Fluorescence; Models, Chemical; Neurotoxins - chemistry; Neurotoxins - toxicity; PC12 Cells; Peptide Fragments - chemistry; Peptide Fragments - ultrastructure; Physiological aspects; Protein Folding; Protein Structure; Protein Structure, Secondary; Rats; Structure; Thiazoles; United States

Diffusible subfibrillar aggregates of amyloid proteins are potent neurotoxins and primary suspects in amyloid diseases including Alzheimer's disease. Despite widespread interest, the molecular structures of the amyloid intermediates and the conformational conversions in amyloid misfolding are p...