Prediction of hyaluronic acid target on sucrase-isomaltase (SI) with reverse docking and molecular dynamics simulations for inhibitors binding to SI.

Auricularia cornea (E.) polysaccharide is an important component of A. cornea Ehrenb, a white mutant strain of Auricularia with biological activities, such as enhancement of human immune function and cancer prevention. The hyaluronic acids (HAs) are important components of the A. cornea polysacchari...

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Autores principales:	Xiao Li, Keqing Qian, Weiwei Han
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/1ab08699d4a04d8b99c05950928bdd90
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spelling	oai:doaj.org-article:1ab08699d4a04d8b99c05950928bdd902021-12-02T20:08:51ZPrediction of hyaluronic acid target on sucrase-isomaltase (SI) with reverse docking and molecular dynamics simulations for inhibitors binding to SI.1932-620310.1371/journal.pone.0255351https://doaj.org/article/1ab08699d4a04d8b99c05950928bdd902021-01-01T00:00:00Zhttps://doi.org/10.1371/journal.pone.0255351https://doaj.org/toc/1932-6203Auricularia cornea (E.) polysaccharide is an important component of A. cornea Ehrenb, a white mutant strain of Auricularia with biological activities, such as enhancement of human immune function and cancer prevention. The hyaluronic acids (HAs) are important components of the A. cornea polysaccharide and have extremely high medicinal value. In this study, we used HA to search the target protein sucrase-isomaltase (SI). In addition, we also performed molecular dynamics (MD) simulations to explore the binding of three inhibitors (HA, acarbose and kotalanol) to SI. The MD simulations indicated that the binding of the three inhibitors may induce the partial disappearance of α helix in residues 530-580. Hence, the hydrogen bond for Gly570-Asn572, which was near the catalytic base Asp471 in SI, was broken during the binding of the three inhibitors. We reveal a new inhibitor for SI and provide reasonable theoretical clues for inhibitor binding to SI.Xiao LiKeqing QianWeiwei HanPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 16, Iss 7, p e0255351 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Xiao Li Keqing Qian Weiwei Han Prediction of hyaluronic acid target on sucrase-isomaltase (SI) with reverse docking and molecular dynamics simulations for inhibitors binding to SI.
description	Auricularia cornea (E.) polysaccharide is an important component of A. cornea Ehrenb, a white mutant strain of Auricularia with biological activities, such as enhancement of human immune function and cancer prevention. The hyaluronic acids (HAs) are important components of the A. cornea polysaccharide and have extremely high medicinal value. In this study, we used HA to search the target protein sucrase-isomaltase (SI). In addition, we also performed molecular dynamics (MD) simulations to explore the binding of three inhibitors (HA, acarbose and kotalanol) to SI. The MD simulations indicated that the binding of the three inhibitors may induce the partial disappearance of α helix in residues 530-580. Hence, the hydrogen bond for Gly570-Asn572, which was near the catalytic base Asp471 in SI, was broken during the binding of the three inhibitors. We reveal a new inhibitor for SI and provide reasonable theoretical clues for inhibitor binding to SI.
format	article
author	Xiao Li Keqing Qian Weiwei Han
author_facet	Xiao Li Keqing Qian Weiwei Han
author_sort	Xiao Li
title	Prediction of hyaluronic acid target on sucrase-isomaltase (SI) with reverse docking and molecular dynamics simulations for inhibitors binding to SI.
title_short	Prediction of hyaluronic acid target on sucrase-isomaltase (SI) with reverse docking and molecular dynamics simulations for inhibitors binding to SI.
title_full	Prediction of hyaluronic acid target on sucrase-isomaltase (SI) with reverse docking and molecular dynamics simulations for inhibitors binding to SI.
title_fullStr	Prediction of hyaluronic acid target on sucrase-isomaltase (SI) with reverse docking and molecular dynamics simulations for inhibitors binding to SI.
title_full_unstemmed	Prediction of hyaluronic acid target on sucrase-isomaltase (SI) with reverse docking and molecular dynamics simulations for inhibitors binding to SI.
title_sort	prediction of hyaluronic acid target on sucrase-isomaltase (si) with reverse docking and molecular dynamics simulations for inhibitors binding to si.
publisher	Public Library of Science (PLoS)
publishDate	2021
url	https://doaj.org/article/1ab08699d4a04d8b99c05950928bdd90
work_keys_str_mv	AT xiaoli predictionofhyaluronicacidtargetonsucraseisomaltasesiwithreversedockingandmoleculardynamicssimulationsforinhibitorsbindingtosi AT keqingqian predictionofhyaluronicacidtargetonsucraseisomaltasesiwithreversedockingandmoleculardynamicssimulationsforinhibitorsbindingtosi AT weiweihan predictionofhyaluronicacidtargetonsucraseisomaltasesiwithreversedockingandmoleculardynamicssimulationsforinhibitorsbindingtosi
_version_	1718375108163141632

Prediction of hyaluronic acid target on sucrase-isomaltase (SI) with reverse docking and molecular dynamics simulations for inhibitors binding to SI.

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