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

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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Main Authors: Xiao Li, Keqing Qian, Weiwei Han
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2021-01-01
Series:PLoS ONE
Online Access:https://doi.org/10.1371/journal.pone.0255351
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spelling doaj-1ab08699d4a04d8b99c05950928bdd902021-08-04T04:30:40ZengPublic Library of Science (PLoS)PLoS ONE1932-62032021-01-01167e025535110.1371/journal.pone.0255351Prediction of hyaluronic acid target on sucrase-isomaltase (SI) with reverse docking and molecular dynamics simulations for inhibitors binding to SI.Xiao LiKeqing QianWeiwei HanAuricularia 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.https://doi.org/10.1371/journal.pone.0255351
collection DOAJ
language English
format Article
sources DOAJ
author Xiao Li
Keqing Qian
Weiwei Han
spellingShingle 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.
PLoS ONE
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)
series PLoS ONE
issn 1932-6203
publishDate 2021-01-01
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.
url https://doi.org/10.1371/journal.pone.0255351
work_keys_str_mv AT xiaoli predictionofhyaluronicacidtargetonsucraseisomaltasesiwithreversedockingandmoleculardynamicssimulationsforinhibitorsbindingtosi
AT keqingqian predictionofhyaluronicacidtargetonsucraseisomaltasesiwithreversedockingandmoleculardynamicssimulationsforinhibitorsbindingtosi
AT weiweihan predictionofhyaluronicacidtargetonsucraseisomaltasesiwithreversedockingandmoleculardynamicssimulationsforinhibitorsbindingtosi
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