Cargando…

EGCG impedes human Tau aggregation and interacts with Tau

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 (EGC...

Descripción completa

Detalles Bibliográficos
Autores principales: Sonawane, Shweta Kishor, Chidambaram, Hariharakrishnan, Boral, Debjyoti, Gorantla, Nalini Vijay, Balmik, Abhishek Ankur, Dangi, Abha, Ramasamy, Sureshkumar, Marelli, Udaya Kiran, Chinnathambi, Subashchandrabose
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7387440/
https://www.ncbi.nlm.nih.gov/pubmed/32724104
http://dx.doi.org/10.1038/s41598-020-69429-6
Descripción
Sumario: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.