Kinetics of Amyloid β Monomer-to-Oligomer Exchange by NMR Relaxation

• Published in: Journal of the American Chemical Society Vol. 132; no. 29; pp. 9948 - 9951
• Main Authors: Fawzi, Nicolas L, Ying, Jinfa, Torchia, Dennis A, Clore, G. Marius
• Format: Journal Article
• Language: English
• Published: United States American Chemical Society 28.07.2010
• Subjects: Amyloid beta-Peptides - chemistry; Amyloid beta-Peptides - metabolism; Buffers; Kinetics; Models, Molecular; Nuclear Magnetic Resonance, Biomolecular; Peptide Fragments - chemistry; Peptide Fragments - metabolism; Protein Multimerization; Protein Structure, Quaternary; Solutions

Recent studies have implicated non-fibrillar oligomers of the amyloid β (Aβ) peptide as the primary toxic species in Alzheimer’s disease. Detailed structural and kinetic characterization of these states, however, has been difficult. Here we use NMR relaxation measurements to address the kinetics of...