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 Lettjournal_title
FEBS lettersauthors
Wobst HJ,Sharma A,Diamond MI,Wanker EE,Bieschke Jdoi
10.1016/j.febslet.2014.11.026subject
Has Abstractpub_date
2015-01-02 00:00:00pages
77-83issue
1eissn
0014-5793issn
1873-3468pii
S0014-5793(14)00831-Xjournal_volume
589pub_type
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