The Potential Role of Rosmarinic Acid and Sinensetin as α-Amylase Inhibitor: In Silico Study

The study of natural compound as α-amylase inhibitor has been a concern since the synthetic drugs for the management of type 2 diabetes mellitus have several side effects. The present study was carried out to predict the ability of rosmarinic acid and sinensetin as human α-amylase inhibitor by in si...

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Autores principales:	Hazna Noor Meidinna, Fatchiyah Fatchiyah
Formato:	article
Lenguaje:	EN
Publicado:	University of Brawijaya 2019
Materias:	α-amylase inhibitor in silico rosmarinic acid sinensetin Chemistry QD1-999
Acceso en línea:	http://dx.doi.org/10.21776/ub.jpacr.2019.008.01.460 https://doaj.org/article/d34c8d2f98474a9d961741c35c94e1bb
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spelling	oai:doaj.org-article:d34c8d2f98474a9d961741c35c94e1bb2021-12-02T13:13:54ZThe Potential Role of Rosmarinic Acid and Sinensetin as α-Amylase Inhibitor: In Silico Studyhttp://dx.doi.org/10.21776/ub.jpacr.2019.008.01.4602302-46902302-4690https://doaj.org/article/d34c8d2f98474a9d961741c35c94e1bb2019-01-01T00:00:00Zhttps://jpacr.ub.ac.id/index.php/jpacr/article/view/460/pdfhttps://doaj.org/toc/2302-4690https://doaj.org/toc/2302-4690The study of natural compound as α-amylase inhibitor has been a concern since the synthetic drugs for the management of type 2 diabetes mellitus have several side effects. The present study was carried out to predict the ability of rosmarinic acid and sinensetin as human α-amylase inhibitor by in silico study. All of the prepared 3D structures were used in the molecular docking by using Hex 8.0.0. The visualization of the molecular interactions of those compounds with human salivary α-amylase or human pancreatic α-amylase was established in the Discovery Studio Client 4.1 software. The result of this study determined that rosmarinic acid and sinensetin bound to the A domain of human pancreatic α-amylase and human salivary α-amylase. Rosmarinic acid-human salivary α-amylase complex was observed to possess high number of hydrogen bonds compared to sinensetin-human salivary α-amylase complex. The similar result was observed in the comparison of rosmarinic acid-human pancreatic α-amylase complex and sinensetin-human pancreatic α-amylase complex. The rosmarinic acid was able to bind the Glu233 of human pancreatic α-amylase. These data suggest rosmarinic acid as a potential inhibitor of human salivary α-amylase and human pancreatic α-amylase. Further experimental evidence is needed to confirm this observation. Hazna Noor MeidinnaFatchiyah FatchiyahUniversity of Brawijayaarticleα-amylase inhibitorin silicorosmarinic acidsinensetinChemistryQD1-999ENJournal of Pure and Applied Chemistry Research, Vol 8, Iss 1, Pp 73-79 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	α-amylase inhibitor in silico rosmarinic acid sinensetin Chemistry QD1-999
spellingShingle	α-amylase inhibitor in silico rosmarinic acid sinensetin Chemistry QD1-999 Hazna Noor Meidinna Fatchiyah Fatchiyah The Potential Role of Rosmarinic Acid and Sinensetin as α-Amylase Inhibitor: In Silico Study
description	The study of natural compound as α-amylase inhibitor has been a concern since the synthetic drugs for the management of type 2 diabetes mellitus have several side effects. The present study was carried out to predict the ability of rosmarinic acid and sinensetin as human α-amylase inhibitor by in silico study. All of the prepared 3D structures were used in the molecular docking by using Hex 8.0.0. The visualization of the molecular interactions of those compounds with human salivary α-amylase or human pancreatic α-amylase was established in the Discovery Studio Client 4.1 software. The result of this study determined that rosmarinic acid and sinensetin bound to the A domain of human pancreatic α-amylase and human salivary α-amylase. Rosmarinic acid-human salivary α-amylase complex was observed to possess high number of hydrogen bonds compared to sinensetin-human salivary α-amylase complex. The similar result was observed in the comparison of rosmarinic acid-human pancreatic α-amylase complex and sinensetin-human pancreatic α-amylase complex. The rosmarinic acid was able to bind the Glu233 of human pancreatic α-amylase. These data suggest rosmarinic acid as a potential inhibitor of human salivary α-amylase and human pancreatic α-amylase. Further experimental evidence is needed to confirm this observation.
format	article
author	Hazna Noor Meidinna Fatchiyah Fatchiyah
author_facet	Hazna Noor Meidinna Fatchiyah Fatchiyah
author_sort	Hazna Noor Meidinna
title	The Potential Role of Rosmarinic Acid and Sinensetin as α-Amylase Inhibitor: In Silico Study
title_short	The Potential Role of Rosmarinic Acid and Sinensetin as α-Amylase Inhibitor: In Silico Study
title_full	The Potential Role of Rosmarinic Acid and Sinensetin as α-Amylase Inhibitor: In Silico Study
title_fullStr	The Potential Role of Rosmarinic Acid and Sinensetin as α-Amylase Inhibitor: In Silico Study
title_full_unstemmed	The Potential Role of Rosmarinic Acid and Sinensetin as α-Amylase Inhibitor: In Silico Study
title_sort	potential role of rosmarinic acid and sinensetin as α-amylase inhibitor: in silico study
publisher	University of Brawijaya
publishDate	2019
url	http://dx.doi.org/10.21776/ub.jpacr.2019.008.01.460 https://doaj.org/article/d34c8d2f98474a9d961741c35c94e1bb
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The Potential Role of Rosmarinic Acid and Sinensetin as α-Amylase Inhibitor: In Silico Study

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