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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...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2020
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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 |
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author | Sonawane, Shweta Kishor Chidambaram, Hariharakrishnan Boral, Debjyoti Gorantla, Nalini Vijay Balmik, Abhishek Ankur Dangi, Abha Ramasamy, Sureshkumar Marelli, Udaya Kiran Chinnathambi, Subashchandrabose |
author_facet | Sonawane, Shweta Kishor Chidambaram, Hariharakrishnan Boral, Debjyoti Gorantla, Nalini Vijay Balmik, Abhishek Ankur Dangi, Abha Ramasamy, Sureshkumar Marelli, Udaya Kiran Chinnathambi, Subashchandrabose |
author_sort | Sonawane, Shweta Kishor |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-7387440 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-73874402020-07-29 EGCG impedes human Tau aggregation and interacts with Tau Sonawane, Shweta Kishor Chidambaram, Hariharakrishnan Boral, Debjyoti Gorantla, Nalini Vijay Balmik, Abhishek Ankur Dangi, Abha Ramasamy, Sureshkumar Marelli, Udaya Kiran Chinnathambi, Subashchandrabose Sci Rep Article 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. Nature Publishing Group UK 2020-07-28 /pmc/articles/PMC7387440/ /pubmed/32724104 http://dx.doi.org/10.1038/s41598-020-69429-6 Text en © The Author(s) 2020 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Sonawane, Shweta Kishor Chidambaram, Hariharakrishnan Boral, Debjyoti Gorantla, Nalini Vijay Balmik, Abhishek Ankur Dangi, Abha Ramasamy, Sureshkumar Marelli, Udaya Kiran Chinnathambi, Subashchandrabose EGCG impedes human Tau aggregation and interacts with Tau |
title | EGCG impedes human Tau aggregation and interacts with Tau |
title_full | EGCG impedes human Tau aggregation and interacts with Tau |
title_fullStr | EGCG impedes human Tau aggregation and interacts with Tau |
title_full_unstemmed | EGCG impedes human Tau aggregation and interacts with Tau |
title_short | EGCG impedes human Tau aggregation and interacts with Tau |
title_sort | egcg impedes human tau aggregation and interacts with tau |
topic | Article |
url | 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 |
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