EGCG remodels mature alpha-synuclein and amyloid-beta fibrils and reduces cellular toxicity.

@article{Bieschke2010EGCGRM,
  title={EGCG remodels mature alpha-synuclein and amyloid-beta fibrils and reduces cellular toxicity.},
  author={Jan Bieschke and Jenny Russ and Ralf Philipp Friedrich and Dagmar E Ehrnhoefer and Heike Julia Wobst and Katja Neugebauer and Erich E. Wanker},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2010},
  volume={107 17},
  pages={7710-5}
}
Protein misfolding and formation of beta-sheet-rich amyloid fibrils or aggregates is related to cellular toxicity and decay in various human disorders including Alzheimer's and Parkinson's disease. Recently, we demonstrated that the polyphenol (-)-epi-gallocatechine gallate (EGCG) inhibits alpha-synuclein and amyloid-beta fibrillogenesis. It associates with natively unfolded polypeptides and promotes the self-assembly of unstructured oligomers of a new type. Whether EGCG disassembles preformed… CONTINUE READING
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