The green tea polyphenol (-)-epigallocatechin gallate prevents the aggregation of tau protein into toxic oligomers at substoichiometric ratios

Item Type:	Article
Title:	The green tea polyphenol (-)-epigallocatechin gallate prevents the aggregation of tau protein into toxic oligomers at substoichiometric ratios
Creators Name:	Wobst, H.J. and Sharma, A. and Diamond, M.I. and Wanker, E.E. and Bieschke, J.
Abstract:	The accumulation of amyloid-beta (Abeta) and tau aggregates is a pathological hallmark of Alzheimer's disease. Both polypeptides form fibrillar deposits, but several lines of evidence indicate that Abeta and tau form toxic oligomeric aggregation intermediates. Depleting such structures could thus be a powerful therapeutic strategy. We generated a fragment of tau (His-K18DeltaK280) that forms stable, toxic, oligomeric tau aggregates in vitro. We show that (-)-epigallocatechin gallate (EGCG), a green tea polyphenol that was previously found to reduce Abeta aggregation, inhibits the aggregation of tau K18DeltaK280 into toxic oligomers at ten- to hundred-fold substoichiometric concentrations, thereby rescuing toxicity in neuronal model cells.
Keywords:	Tau Protein, Tau Oligomers, Aggregation Inhibitors, EGCG, Alzheimer's Disease, Polyphenol, Animals, Rats
Source:	FEBS Letters
ISSN:	0014-5793
Publisher:	Wiley-Blackwell
Volume:	589
Number:	1
Page Range:	77-83
Date:	2 January 2015
Official Publication:	https://doi.org/10.1016/j.febslet.2014.11.026
PubMed:	View item in PubMed

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