Inhibition mechanism of SARS-CoV-2 main protease by ebselen and its derivatives

Ebselen is an organoselenium drug that inhibits the SARS-CoV-2 main protease (Mpro). Here, the authors co-crystallised Mpro with ebselen and an ebselen derivative and observed an enzyme bound organoselenium covalent adduct in the crystal structures, which was also confirmed by mass spectrometry anal...

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Autores principales:	Kangsa Amporndanai, Xiaoli Meng, Weijuan Shang, Zhenmig Jin, Michael Rogers, Yao Zhao, Zihe Rao, Zhi-Jie Liu, Haitao Yang, Leike Zhang, Paul M. O’Neill, S. Samar Hasnain
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/8cf917f0f0d94c58998c45d6d9518f5b
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spelling	oai:doaj.org-article:8cf917f0f0d94c58998c45d6d9518f5b2021-12-02T14:49:16ZInhibition mechanism of SARS-CoV-2 main protease by ebselen and its derivatives10.1038/s41467-021-23313-72041-1723https://doaj.org/article/8cf917f0f0d94c58998c45d6d9518f5b2021-05-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-23313-7https://doaj.org/toc/2041-1723Ebselen is an organoselenium drug that inhibits the SARS-CoV-2 main protease (Mpro). Here, the authors co-crystallised Mpro with ebselen and an ebselen derivative and observed an enzyme bound organoselenium covalent adduct in the crystal structures, which was also confirmed by mass spectrometry analysis.Kangsa AmporndanaiXiaoli MengWeijuan ShangZhenmig JinMichael RogersYao ZhaoZihe RaoZhi-Jie LiuHaitao YangLeike ZhangPaul M. O’NeillS. Samar HasnainNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-7 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Kangsa Amporndanai Xiaoli Meng Weijuan Shang Zhenmig Jin Michael Rogers Yao Zhao Zihe Rao Zhi-Jie Liu Haitao Yang Leike Zhang Paul M. O’Neill S. Samar Hasnain Inhibition mechanism of SARS-CoV-2 main protease by ebselen and its derivatives
description	Ebselen is an organoselenium drug that inhibits the SARS-CoV-2 main protease (Mpro). Here, the authors co-crystallised Mpro with ebselen and an ebselen derivative and observed an enzyme bound organoselenium covalent adduct in the crystal structures, which was also confirmed by mass spectrometry analysis.
format	article
author	Kangsa Amporndanai Xiaoli Meng Weijuan Shang Zhenmig Jin Michael Rogers Yao Zhao Zihe Rao Zhi-Jie Liu Haitao Yang Leike Zhang Paul M. O’Neill S. Samar Hasnain
author_facet	Kangsa Amporndanai Xiaoli Meng Weijuan Shang Zhenmig Jin Michael Rogers Yao Zhao Zihe Rao Zhi-Jie Liu Haitao Yang Leike Zhang Paul M. O’Neill S. Samar Hasnain
author_sort	Kangsa Amporndanai
title	Inhibition mechanism of SARS-CoV-2 main protease by ebselen and its derivatives
title_short	Inhibition mechanism of SARS-CoV-2 main protease by ebselen and its derivatives
title_full	Inhibition mechanism of SARS-CoV-2 main protease by ebselen and its derivatives
title_fullStr	Inhibition mechanism of SARS-CoV-2 main protease by ebselen and its derivatives
title_full_unstemmed	Inhibition mechanism of SARS-CoV-2 main protease by ebselen and its derivatives
title_sort	inhibition mechanism of sars-cov-2 main protease by ebselen and its derivatives
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/8cf917f0f0d94c58998c45d6d9518f5b
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Inhibition mechanism of SARS-CoV-2 main protease by ebselen and its derivatives

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