| Literature DB >> 24157371 |
Yanqin Liu1, Tara L Pukala, Ian F Musgrave, Danielle M Williams, Francis C Dehle, John A Carver.
Abstract
Many protein misfolding diseases, for example, Alzheimer's, Parkinson's and Huntington's, are characterised by the accumulation of protein aggregates in an amyloid fibrillar form. Natural products which inhibit fibril formation are a promising avenue to explore as therapeutics for the treatment of these diseases. In this study we have shown, using in vitro thioflavin T assays and transmission electron microscopy, that grape seed extract inhibits fibril formation of kappa-casein (κ-CN), a milk protein which forms amyloid fibrils spontaneously under physiological conditions. Among the components of grape seed extract, gallic acid was the most active component at inhibiting κ-CN fibril formation, by stabilizing κ-CN to prevent its aggregation. Concomitantly, gallic acid significantly reduced the toxicity of κ-CN to pheochromocytoma12 cells. Furthermore, gallic acid effectively inhibited fibril formation by the amyloid-beta peptide, the putative causative agent in Alzheimer's disease. It is concluded that the gallate moiety has the fibril-inhibitory activity.Entities:
Keywords: 1,4-dithiothreitol; 3-[4,5-dimethylthiazol-2-yl]-2,5-diphenyltetrazolium bromide; AD; Alzheimer’s disease; Amyloid fibril; Amyloid-beta peptide; Aβ; DTT; EGCG; GA; GSE; Gallic acid; Grape seed extract; HD; Huntington’s disease; Kappa-casein; MTT; PC12; PD; Parkinson’s disease; Protein aggregation; RCM-κ-CN; TEM; ThT; Thioflavin T; amyloid-beta peptide; epigallocatechin-3-gallate; gallic acid; grape seed extract; pheochromocytoma12; reduced and carboxymethylated kappa-casein; transmission electron microscopy
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Year: 2013 PMID: 24157371 DOI: 10.1016/j.bmcl.2013.09.071
Source DB: PubMed Journal: Bioorg Med Chem Lett ISSN: 0960-894X Impact factor: 2.823