Inhibition of gut bacterial β-glucuronidase by chemical components from black tea: Inhibition interactions and molecular mechanism

Gut bacterial β-glucuronidase is regarded as an important molecular target for several therapeutic applications. Inhibitors of β-glucuronidase can effectively alleviate the drug-induced gastrointestinal tract toxicity. In this study, the ethanol extracts of black tea was found to display significant...

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Autores principales:	Cheng-Peng Sun, Xiang-Ge Tian, Lei Feng, Chao Wang, Jing-Xin Li, Xiao-Kui Huo, Wen-Yu Zhao, Jing Ning, Zhen-Long Yu, Sa Deng, Bao-Jing Zhang, Xia Lv, Jie Hou, Xiao-Chi Ma
Formato:	article
Lenguaje:	EN
Publicado:	Elsevier 2021
Materias:	β-glucuronidase Catechins Theaflavins Inhibitory kinetics Molecular simulation Chemistry QD1-999
Acceso en línea:	https://doaj.org/article/99f3e1c8597e440ba0d673c8006141b0
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spelling	oai:doaj.org-article:99f3e1c8597e440ba0d673c8006141b02021-11-20T04:58:14ZInhibition of gut bacterial β-glucuronidase by chemical components from black tea: Inhibition interactions and molecular mechanism1878-535210.1016/j.arabjc.2021.103457https://doaj.org/article/99f3e1c8597e440ba0d673c8006141b02021-12-01T00:00:00Zhttp://www.sciencedirect.com/science/article/pii/S187853522100472Xhttps://doaj.org/toc/1878-5352Gut bacterial β-glucuronidase is regarded as an important molecular target for several therapeutic applications. Inhibitors of β-glucuronidase can effectively alleviate the drug-induced gastrointestinal tract toxicity. In this study, the ethanol extracts of black tea was found to display significant inhibitory activities against Escherichia coli β-glucuronidase (EcGUS), and seven polyphenols including catechins and theaflavins were identified as the key components responsible for the strong inhibitory potency of black tea towards EcGUS. Among these seven identified naturally occurring inhibitors, (−)-catechin gallate (CG), theaflavin-3-monogallate (TF-3-G), theaflavin-3′-monogallate (TF-3′-G) and theaflavin-3,3′-digallate (TFDG) were more potent inhibitors of EcGUS compared with (−)-epicatechin gallate (ECG), (−)-gallocatechin gallate (GCG), and (−)-epigallocatechin gallate (EGCG). Furthermore, molecular docking and molecular dynamics simulation results further indicated that TFDG could bind in the cavity of EcGUS and interacted with key residues Ser360, Glu413 and Ile560 of EcGUS through hydrogen bonds. Taken together, these data offer important information for efficient development of black tea and its catechins and theaflavins constituents for treating drug-induced enteropathy.Cheng-Peng SunXiang-Ge TianLei FengChao WangJing-Xin LiXiao-Kui HuoWen-Yu ZhaoJing NingZhen-Long YuSa DengBao-Jing ZhangXia LvJie HouXiao-Chi MaElsevierarticleβ-glucuronidaseCatechinsTheaflavinsInhibitory kineticsMolecular simulationChemistryQD1-999ENArabian Journal of Chemistry, Vol 14, Iss 12, Pp 103457- (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	β-glucuronidase Catechins Theaflavins Inhibitory kinetics Molecular simulation Chemistry QD1-999
spellingShingle	β-glucuronidase Catechins Theaflavins Inhibitory kinetics Molecular simulation Chemistry QD1-999 Cheng-Peng Sun Xiang-Ge Tian Lei Feng Chao Wang Jing-Xin Li Xiao-Kui Huo Wen-Yu Zhao Jing Ning Zhen-Long Yu Sa Deng Bao-Jing Zhang Xia Lv Jie Hou Xiao-Chi Ma Inhibition of gut bacterial β-glucuronidase by chemical components from black tea: Inhibition interactions and molecular mechanism
description	Gut bacterial β-glucuronidase is regarded as an important molecular target for several therapeutic applications. Inhibitors of β-glucuronidase can effectively alleviate the drug-induced gastrointestinal tract toxicity. In this study, the ethanol extracts of black tea was found to display significant inhibitory activities against Escherichia coli β-glucuronidase (EcGUS), and seven polyphenols including catechins and theaflavins were identified as the key components responsible for the strong inhibitory potency of black tea towards EcGUS. Among these seven identified naturally occurring inhibitors, (−)-catechin gallate (CG), theaflavin-3-monogallate (TF-3-G), theaflavin-3′-monogallate (TF-3′-G) and theaflavin-3,3′-digallate (TFDG) were more potent inhibitors of EcGUS compared with (−)-epicatechin gallate (ECG), (−)-gallocatechin gallate (GCG), and (−)-epigallocatechin gallate (EGCG). Furthermore, molecular docking and molecular dynamics simulation results further indicated that TFDG could bind in the cavity of EcGUS and interacted with key residues Ser360, Glu413 and Ile560 of EcGUS through hydrogen bonds. Taken together, these data offer important information for efficient development of black tea and its catechins and theaflavins constituents for treating drug-induced enteropathy.
format	article
author	Cheng-Peng Sun Xiang-Ge Tian Lei Feng Chao Wang Jing-Xin Li Xiao-Kui Huo Wen-Yu Zhao Jing Ning Zhen-Long Yu Sa Deng Bao-Jing Zhang Xia Lv Jie Hou Xiao-Chi Ma
author_facet	Cheng-Peng Sun Xiang-Ge Tian Lei Feng Chao Wang Jing-Xin Li Xiao-Kui Huo Wen-Yu Zhao Jing Ning Zhen-Long Yu Sa Deng Bao-Jing Zhang Xia Lv Jie Hou Xiao-Chi Ma
author_sort	Cheng-Peng Sun
title	Inhibition of gut bacterial β-glucuronidase by chemical components from black tea: Inhibition interactions and molecular mechanism
title_short	Inhibition of gut bacterial β-glucuronidase by chemical components from black tea: Inhibition interactions and molecular mechanism
title_full	Inhibition of gut bacterial β-glucuronidase by chemical components from black tea: Inhibition interactions and molecular mechanism
title_fullStr	Inhibition of gut bacterial β-glucuronidase by chemical components from black tea: Inhibition interactions and molecular mechanism
title_full_unstemmed	Inhibition of gut bacterial β-glucuronidase by chemical components from black tea: Inhibition interactions and molecular mechanism
title_sort	inhibition of gut bacterial β-glucuronidase by chemical components from black tea: inhibition interactions and molecular mechanism
publisher	Elsevier
publishDate	2021
url	https://doaj.org/article/99f3e1c8597e440ba0d673c8006141b0
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Inhibition of gut bacterial β-glucuronidase by chemical components from black tea: Inhibition interactions and molecular mechanism

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