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

Abstract:

:The accumulation of amyloid-beta (Aβ) and tau aggregates is a pathological hallmark of Alzheimer's disease. Both polypeptides form fibrillar deposits, but several lines of evidence indicate that Aβ and tau form toxic oligomeric aggregation intermediates. Depleting such structures could thus be a powerful therapeutic strategy. We generated a fragment of tau (His-K18ΔK280) 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 Aβ aggregation, inhibits the aggregation of tau K18ΔK280 into toxic oligomers at ten- to hundred-fold substoichiometric concentrations, thereby rescuing toxicity in neuronal model cells.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Wobst HJ,Sharma A,Diamond MI,Wanker EE,Bieschke J

doi

10.1016/j.febslet.2014.11.026

subject

Has Abstract

pub_date

2015-01-02 00:00:00

pages

77-83

issue

1

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(14)00831-X

journal_volume

589

pub_type

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