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

Heike J. Wobst, Apurwa Sharma, Marc I. Diamond, Erich E. Wanker, Jan Bieschke

Research output: Contribution to journalArticle

72 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)77-83
Number of pages7
JournalFEBS Letters
Volume589
Issue number1
DOIs
StatePublished - Feb 2 2015

Keywords

  • (-)-Epigallocatechin gallate
  • Aggregation inhibitors
  • Alzheimers disease
  • Polyphenol
  • Tau oligomers
  • Tau protein

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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