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Flavonoids as Human Intestinal α-Glucosidase Inhibitors
Certain flavonoids can influence glucose metabolism by inhibiting enzymes involved in carbohydrate digestion and suppressing intestinal glucose absorption. In this study, four structurally-related flavonols (quercetin, kaempferol, quercetagetin and galangin) were evaluated individually for their abi...
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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MDPI
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8392382/ https://www.ncbi.nlm.nih.gov/pubmed/34441720 http://dx.doi.org/10.3390/foods10081939 |
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author | Barber, Elizabeth Houghton, Michael J. Williamson, Gary |
author_facet | Barber, Elizabeth Houghton, Michael J. Williamson, Gary |
author_sort | Barber, Elizabeth |
collection | PubMed |
description | Certain flavonoids can influence glucose metabolism by inhibiting enzymes involved in carbohydrate digestion and suppressing intestinal glucose absorption. In this study, four structurally-related flavonols (quercetin, kaempferol, quercetagetin and galangin) were evaluated individually for their ability to inhibit human α-glucosidases (sucrase, maltase and isomaltase), and were compared with the antidiabetic drug acarbose and the flavan-3-ol(−)-epigallocatechin-3-gallate (EGCG). Cell-free extracts from human intestinal Caco-2/TC7 cells were used as the enzyme source and products were quantified chromatographically with high accuracy, precision and sensitivity. Acarbose inhibited sucrase, maltase and isomaltase with IC(50) values of 1.65, 13.9 and 39.1 µM, respectively. A similar inhibition pattern, but with comparatively higher values, was observed with EGCG. Of the flavonols, quercetagetin was the strongest inhibitor of α-glucosidases, with inhibition constants approaching those of acarbose, followed by galangin and kaempferol, while the weakest were quercetin and EGCG. The varied inhibitory effects of flavonols against human α-glucosidases depend on their structures, the enzyme source and substrates employed. The flavonols were more effective than EGCG, but less so than acarbose, and so may be useful in regulating sugar digestion and postprandial glycaemia without the side effects associated with acarbose treatment. |
format | Online Article Text |
id | pubmed-8392382 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-83923822021-08-28 Flavonoids as Human Intestinal α-Glucosidase Inhibitors Barber, Elizabeth Houghton, Michael J. Williamson, Gary Foods Article Certain flavonoids can influence glucose metabolism by inhibiting enzymes involved in carbohydrate digestion and suppressing intestinal glucose absorption. In this study, four structurally-related flavonols (quercetin, kaempferol, quercetagetin and galangin) were evaluated individually for their ability to inhibit human α-glucosidases (sucrase, maltase and isomaltase), and were compared with the antidiabetic drug acarbose and the flavan-3-ol(−)-epigallocatechin-3-gallate (EGCG). Cell-free extracts from human intestinal Caco-2/TC7 cells were used as the enzyme source and products were quantified chromatographically with high accuracy, precision and sensitivity. Acarbose inhibited sucrase, maltase and isomaltase with IC(50) values of 1.65, 13.9 and 39.1 µM, respectively. A similar inhibition pattern, but with comparatively higher values, was observed with EGCG. Of the flavonols, quercetagetin was the strongest inhibitor of α-glucosidases, with inhibition constants approaching those of acarbose, followed by galangin and kaempferol, while the weakest were quercetin and EGCG. The varied inhibitory effects of flavonols against human α-glucosidases depend on their structures, the enzyme source and substrates employed. The flavonols were more effective than EGCG, but less so than acarbose, and so may be useful in regulating sugar digestion and postprandial glycaemia without the side effects associated with acarbose treatment. MDPI 2021-08-20 /pmc/articles/PMC8392382/ /pubmed/34441720 http://dx.doi.org/10.3390/foods10081939 Text en © 2021 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 Barber, Elizabeth Houghton, Michael J. Williamson, Gary Flavonoids as Human Intestinal α-Glucosidase Inhibitors |
title | Flavonoids as Human Intestinal α-Glucosidase Inhibitors |
title_full | Flavonoids as Human Intestinal α-Glucosidase Inhibitors |
title_fullStr | Flavonoids as Human Intestinal α-Glucosidase Inhibitors |
title_full_unstemmed | Flavonoids as Human Intestinal α-Glucosidase Inhibitors |
title_short | Flavonoids as Human Intestinal α-Glucosidase Inhibitors |
title_sort | flavonoids as human intestinal α-glucosidase inhibitors |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8392382/ https://www.ncbi.nlm.nih.gov/pubmed/34441720 http://dx.doi.org/10.3390/foods10081939 |
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