EGCG impedes human Tau aggregation and interacts with Tau

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作者
Shweta Kishor Sonawane
Hariharakrishnan Chidambaram
Debjyoti Boral
Nalini Vijay Gorantla
Abhishek Ankur Balmik
Abha Dangi
Sureshkumar Ramasamy
Udaya Kiran Marelli
Subashchandrabose Chinnathambi
机构
[1] CSIR-National Chemical Laboratory,Neurobiology Group, Division of Biochemical Sciences
[2] CSIR-National Chemical Laboratory,Structural Biology Group, Division of Biochemical Sciences
[3] CSIR-National Chemical Laboratory,Central NMR Facility and Division of Organic Chemistry
[4] Academy of Scientific and Innovative Research (AcSIR),undefined
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Tau aggregation and accumulation is a key event in the pathogenesis of Alzheimer’s disease. Inhibition of Tau aggregation is therefore a potential therapeutic strategy to ameliorate the disease. Phytochemicals are being highlighted as potential aggregation inhibitors. Epigallocatechin-3-gallate (EGCG) is an active phytochemical of green tea that has shown its potency against various diseases including aggregation inhibition of repeat Tau. The potency of EGCG in altering the PHF assembly of full-length human Tau has not been fully explored. By various biophysical and biochemical analyses like ThS fluorescence assay, MALDI-TOF analysis and Isothermal Titration Calorimetry, we demonstrate dual effect of EGCG on aggregation inhibition and disassembly of full-length Tau and their binding affinity. The IC50 for Tau aggregation by EGCG was found to be 64.2 μM.
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