3D NMR structure of a complex between the amyloid beta peptide (1–40) and the polyphenol ε-viniferin glucoside: Implications in Alzheimer's disease

• Published in: Biochimica et biophysica acta Vol. 1830; no. 11; pp. 5068 - 5074
• Main Authors: Richard, Tristan, Papastamoulis, Yorgos, Waffo-Teguo, Pierre, Monti, Jean-Pierre
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.11.2013
• Subjects: Alzheimer disease; Alzheimer Disease - metabolism; Alzheimer Disease - pathology; Alzheimer's disease; amyloid; Amyloid beta-Peptides - chemistry; Amyloid beta-Peptides - metabolism; Animals; Benzofurans - chemistry; Benzofurans - metabolism; Binding Sites; cell death; Cell Line, Tumor; Glucosides - chemistry; Glucosides - metabolism; human physiology; Interaction; Magnetic Resonance Spectroscopy - methods; Models, Molecular; molecular models; neurodegenerative diseases; neurotoxicity; NMR; nuclear magnetic resonance spectroscopy; PC12 Cells; Peptide Fragments - chemistry; Peptide Fragments - metabolism; peptides; Polyphenol; polyphenols; Polyphenols - chemistry; Polyphenols - metabolism; protective effect; Protein Conformation; Rats; Stilbenes - chemistry; Stilbenes - metabolism; viniferins; β-amyloid peptide; NMR; Polyphenol; β-amyloid peptide; Alzheimer's disease; Interaction

Alzheimer's disease (AD) is a progressive neurodegenerative disorder. There is a consensus that Aβ is a pathologic agent and that its toxic effects, which are at present incompletely understood, may occur through several potential mechanisms. Polyphenols are known to have wide-ranging propertie...