Protective effect of epsilon-viniferin on beta-amyloid peptide aggregation investigated by electrospray ionization mass spectrometry

作者：Richard Tristan^*; Poupard Pascal; Nassra Merian; Papastamoulis Yorgos; Iglesias Marie Laure; Krisa Stephanie; Waffo Teguo Pierre; Merillon Jean Michel; Monti Jean Pierre

来源：Bioorganic & Medicinal Chemistry, 2011, 19(10): 3152-3155.

DOI：10.1016/j.bmc.2011.04.001

• Alzheimer's disease
• beta-Amyloid peptide
• Polyphenols
• Cytotoxicity
• Mass spectrometry

Abnormal beta-amyloid peptide accumulation and aggregation is considered to be responsible for the formation and cerebral deposition of senile plaques in the brains of patients with Alzheimer's disease (AD). Inhibition of the formation of beta-amyloid (A beta) fibrils would be an attractive therapeutic target for the treatment of AD. Resveratrol and its derivatives exhibit a broad range of pharmacological properties such as protection against cardiovascular diseases and cancers, as well as promoting antiaging effects. We reported previously that epsilon-viniferin glucoside (VG), a resveratrol-derived dimer, strongly inhibits A beta (2535) fibril formation in vitro. In this study, we investigated the effects of VG on the aggregation of the full-length peptides (A beta (1-40) and A beta (1-42)) and on the beta-amyloid-induced toxicity in PC12 cells. VG inhibited Ab cytotoxicity and the non-covalent complex between VG and A beta was observed by electrospray ionization mass spectrometry.

• 出版日期2011-5-15