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Inhibitory evaluation of Curculigo latifolia on α-glucosidase, DPP (IV) and in vitro studies in antidiabetic with molecular docking relevance to type 2 diabetes mellitus

The inhibition of α-glucosidase and DPP enzymes capable of effectively reducing blood glucose level in the management of type 2 diabetes. The purpose of the present study is to evaluate the inhibitory potential of α-glucosidase and DPP (IV) activity including with the 2-NBDG uptake assay and insulin...

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Autores principales: Zabidi, Nur Athirah, Ishak, Nur Akmal, Hamid, Muhajir, Ashari, Siti Efliza, Mohammad Latif, Muhammad Alif
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Taylor & Francis 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7717572/
https://www.ncbi.nlm.nih.gov/pubmed/33249946
http://dx.doi.org/10.1080/14756366.2020.1844680
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author Zabidi, Nur Athirah
Ishak, Nur Akmal
Hamid, Muhajir
Ashari, Siti Efliza
Mohammad Latif, Muhammad Alif
author_facet Zabidi, Nur Athirah
Ishak, Nur Akmal
Hamid, Muhajir
Ashari, Siti Efliza
Mohammad Latif, Muhammad Alif
author_sort Zabidi, Nur Athirah
collection PubMed
description The inhibition of α-glucosidase and DPP enzymes capable of effectively reducing blood glucose level in the management of type 2 diabetes. The purpose of the present study is to evaluate the inhibitory potential of α-glucosidase and DPP (IV) activity including with the 2-NBDG uptake assay and insulin secretion activities through in vitro studies. The selected of active compounds obtained from the screening of compounds by LC-MS were docked with the targeted enzyme that involved in the mechanism of T2DM. From the results, root extracts displayed a better promising outcome in α-glucosidase (IC(50) 2.72 ± 0.32) as compared with the fruit extracts (IC(50) 3.87 ± 0.32). Besides, root extracts also displayed a better activity in the inhibition of DPP (IV), enhance insulin secretion and glucose uptake activity. Molecular docking results revealing that phlorizin binds strongly with α-glucosidase, DPP (IV) and Insulin receptor (IR) enzymes with achieving the lowest binding energy value. The present work suggests several of the compounds have the potential that contribute towards inhibiting α-glucosidase and DPP (IV) and thus effective in lowering post-prandial hyperglycaemia.
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spelling pubmed-77175722020-12-10 Inhibitory evaluation of Curculigo latifolia on α-glucosidase, DPP (IV) and in vitro studies in antidiabetic with molecular docking relevance to type 2 diabetes mellitus Zabidi, Nur Athirah Ishak, Nur Akmal Hamid, Muhajir Ashari, Siti Efliza Mohammad Latif, Muhammad Alif J Enzyme Inhib Med Chem Research Paper The inhibition of α-glucosidase and DPP enzymes capable of effectively reducing blood glucose level in the management of type 2 diabetes. The purpose of the present study is to evaluate the inhibitory potential of α-glucosidase and DPP (IV) activity including with the 2-NBDG uptake assay and insulin secretion activities through in vitro studies. The selected of active compounds obtained from the screening of compounds by LC-MS were docked with the targeted enzyme that involved in the mechanism of T2DM. From the results, root extracts displayed a better promising outcome in α-glucosidase (IC(50) 2.72 ± 0.32) as compared with the fruit extracts (IC(50) 3.87 ± 0.32). Besides, root extracts also displayed a better activity in the inhibition of DPP (IV), enhance insulin secretion and glucose uptake activity. Molecular docking results revealing that phlorizin binds strongly with α-glucosidase, DPP (IV) and Insulin receptor (IR) enzymes with achieving the lowest binding energy value. The present work suggests several of the compounds have the potential that contribute towards inhibiting α-glucosidase and DPP (IV) and thus effective in lowering post-prandial hyperglycaemia. Taylor & Francis 2020-11-29 /pmc/articles/PMC7717572/ /pubmed/33249946 http://dx.doi.org/10.1080/14756366.2020.1844680 Text en © 2020 The Author(s). Published by Informa UK Limited, trading as Taylor & Francis Group. https://creativecommons.org/licenses/by/4.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Paper
Zabidi, Nur Athirah
Ishak, Nur Akmal
Hamid, Muhajir
Ashari, Siti Efliza
Mohammad Latif, Muhammad Alif
Inhibitory evaluation of Curculigo latifolia on α-glucosidase, DPP (IV) and in vitro studies in antidiabetic with molecular docking relevance to type 2 diabetes mellitus
title Inhibitory evaluation of Curculigo latifolia on α-glucosidase, DPP (IV) and in vitro studies in antidiabetic with molecular docking relevance to type 2 diabetes mellitus
title_full Inhibitory evaluation of Curculigo latifolia on α-glucosidase, DPP (IV) and in vitro studies in antidiabetic with molecular docking relevance to type 2 diabetes mellitus
title_fullStr Inhibitory evaluation of Curculigo latifolia on α-glucosidase, DPP (IV) and in vitro studies in antidiabetic with molecular docking relevance to type 2 diabetes mellitus
title_full_unstemmed Inhibitory evaluation of Curculigo latifolia on α-glucosidase, DPP (IV) and in vitro studies in antidiabetic with molecular docking relevance to type 2 diabetes mellitus
title_short Inhibitory evaluation of Curculigo latifolia on α-glucosidase, DPP (IV) and in vitro studies in antidiabetic with molecular docking relevance to type 2 diabetes mellitus
title_sort inhibitory evaluation of curculigo latifolia on α-glucosidase, dpp (iv) and in vitro studies in antidiabetic with molecular docking relevance to type 2 diabetes mellitus
topic Research Paper
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7717572/
https://www.ncbi.nlm.nih.gov/pubmed/33249946
http://dx.doi.org/10.1080/14756366.2020.1844680
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