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https://hdl.handle.net/2440/81696
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Type: | Journal article |
Title: | Gallic acid is the major component of grape seed extract that inhibits amyloid fibril formation |
Author: | Liu, Y. Pukala, T. Musgrave, I. Williams, D. Dehle, F. Carver, J. |
Citation: | Bioorganic and Medicinal Chemistry Letters, 2013; 23(23):6336-6340 |
Publisher: | Pergamon-Elsevier Science Ltd |
Issue Date: | 2013 |
ISSN: | 0960-894X 1464-3405 |
Statement of Responsibility: | Yanqin Liu, 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. |
Keywords: | Amyloid fibril Grape seed extract Gallic acid Kappa-casein Amyloid-beta peptide Protein aggregation |
Rights: | © 2013 Elsevier Ltd. All rights reserved. |
DOI: | 10.1016/j.bmcl.2013.09.071 |
Grant ID: | ARC |
Published version: | http://dx.doi.org/10.1016/j.bmcl.2013.09.071 |
Appears in Collections: | Aurora harvest 4 Chemistry and Physics publications |
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