Epigallocatechin gallate, an antioxidant popularly known as EGCG, can prevent the formation of amyloid fibrils, toxic protein aggregates associated with Alzheimer's and Parkinson's diseases. The findings, published online in Nature Structural & Molecular Biology, may pave the way for the development of more potent compounds designed to prevent amyloid formation associated with several neurodegenerative diseases.
The accumulation of amyloid fibrils in disorders such as Alzheimer's and Parkinson's are believed to be caused by the misfolding and aggregation of certain unfolded proteins, which can be toxic to cells and lead to neurodegeneration. Erich Wanker and colleagues show that EGCG, a compound found abundantly in green tea, can bind to these natively unfolded proteins and prevent their conversion to toxic amyloid species. Instead, EGCG directs them to 'off-pathway' aggregates that are non-harmful to cells.
Because the authors found that EGCG also binds to unfolded proteins not associated with these diseases, future work could be directed to design compounds that specifically recognize the proteins linked to amyloid formation.
Erich Wanker (Max Delbrueck Center for Molecular Medicine, Berlin, Germany)
Abstract available online.
(C) Nature Structural & Molecular Biology press release.
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