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Inhibitory Mechanism of Quercimeritrin as a Novel α-Glucosidase Selective Inhibitor
In this study, 12 flavonoid glycosides were selected based on virtual screening and the literature, and Quercimeritrin was selected as the best selective inhibitor of α-glucosidase through in vitro enzyme activity inhibition experiments. Its IC(50) value for α-glucosidase was 79.88 µM, and its IC(50...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10528180/ https://www.ncbi.nlm.nih.gov/pubmed/37761124 http://dx.doi.org/10.3390/foods12183415 |
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author | Guo, Fengyu An, Jie Wang, Minlong Zhang, Weibo Chen, Chong Mao, Xueying Liu, Siyuan Wang, Pengjie Ren, Fazheng |
author_facet | Guo, Fengyu An, Jie Wang, Minlong Zhang, Weibo Chen, Chong Mao, Xueying Liu, Siyuan Wang, Pengjie Ren, Fazheng |
author_sort | Guo, Fengyu |
collection | PubMed |
description | In this study, 12 flavonoid glycosides were selected based on virtual screening and the literature, and Quercimeritrin was selected as the best selective inhibitor of α-glucosidase through in vitro enzyme activity inhibition experiments. Its IC(50) value for α-glucosidase was 79.88 µM, and its IC(50) value for α-amylase >250 µM. As such, it could be used as a new selective inhibitor of α-glucosidase. The selective inhibition mechanism of Quercimeritrin on the two starch-digesting enzymes was further explored, and it was confirmed that Quercimeritrin had a strong binding affinity for α-glucosidase and occupied the binding pocket of α-glucosidase through non-covalent binding. Subsequently, animal experiments demonstrated that Quercimeritrin can effectively control postprandial blood glucose in vivo, with the same inhibitory effect as acarbose but without side effects. Our results, therefore, provide insights into how flavone aglycones can be used to effectively control the rate of digestion to improve postprandial blood glucose levels. |
format | Online Article Text |
id | pubmed-10528180 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-105281802023-09-28 Inhibitory Mechanism of Quercimeritrin as a Novel α-Glucosidase Selective Inhibitor Guo, Fengyu An, Jie Wang, Minlong Zhang, Weibo Chen, Chong Mao, Xueying Liu, Siyuan Wang, Pengjie Ren, Fazheng Foods Article In this study, 12 flavonoid glycosides were selected based on virtual screening and the literature, and Quercimeritrin was selected as the best selective inhibitor of α-glucosidase through in vitro enzyme activity inhibition experiments. Its IC(50) value for α-glucosidase was 79.88 µM, and its IC(50) value for α-amylase >250 µM. As such, it could be used as a new selective inhibitor of α-glucosidase. The selective inhibition mechanism of Quercimeritrin on the two starch-digesting enzymes was further explored, and it was confirmed that Quercimeritrin had a strong binding affinity for α-glucosidase and occupied the binding pocket of α-glucosidase through non-covalent binding. Subsequently, animal experiments demonstrated that Quercimeritrin can effectively control postprandial blood glucose in vivo, with the same inhibitory effect as acarbose but without side effects. Our results, therefore, provide insights into how flavone aglycones can be used to effectively control the rate of digestion to improve postprandial blood glucose levels. MDPI 2023-09-13 /pmc/articles/PMC10528180/ /pubmed/37761124 http://dx.doi.org/10.3390/foods12183415 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Guo, Fengyu An, Jie Wang, Minlong Zhang, Weibo Chen, Chong Mao, Xueying Liu, Siyuan Wang, Pengjie Ren, Fazheng Inhibitory Mechanism of Quercimeritrin as a Novel α-Glucosidase Selective Inhibitor |
title | Inhibitory Mechanism of Quercimeritrin as a Novel α-Glucosidase Selective Inhibitor |
title_full | Inhibitory Mechanism of Quercimeritrin as a Novel α-Glucosidase Selective Inhibitor |
title_fullStr | Inhibitory Mechanism of Quercimeritrin as a Novel α-Glucosidase Selective Inhibitor |
title_full_unstemmed | Inhibitory Mechanism of Quercimeritrin as a Novel α-Glucosidase Selective Inhibitor |
title_short | Inhibitory Mechanism of Quercimeritrin as a Novel α-Glucosidase Selective Inhibitor |
title_sort | inhibitory mechanism of quercimeritrin as a novel α-glucosidase selective inhibitor |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10528180/ https://www.ncbi.nlm.nih.gov/pubmed/37761124 http://dx.doi.org/10.3390/foods12183415 |
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