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Antidiabetic activity of Commiphora mukul and Phyllanthus emblica and Computational analysis for the identification of active principles with dipeptidyl peptidase IV inhibitory activity

The medicinal plants may serve as natural alternatives to synthetic antidiabetic medications such as dipeptidyl peptidase-IV (DPP-IV) inhibitors, which are commonly prescribed in clinical practise. The medicinal plants: Commiphora mukul and Phyllanthus emblica have considerable DPP-IV inhibitory eff...

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Autores principales: Mohanty, Ipseeta Ray, Kumar, C. Selvaa, Borde, Manjusha
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Wolters Kluwer - Medknow 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8641738/
https://www.ncbi.nlm.nih.gov/pubmed/34854407
http://dx.doi.org/10.4103/ijp.IJP_69_19
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author Mohanty, Ipseeta Ray
Kumar, C. Selvaa
Borde, Manjusha
author_facet Mohanty, Ipseeta Ray
Kumar, C. Selvaa
Borde, Manjusha
author_sort Mohanty, Ipseeta Ray
collection PubMed
description The medicinal plants may serve as natural alternatives to synthetic antidiabetic medications such as dipeptidyl peptidase-IV (DPP-IV) inhibitors, which are commonly prescribed in clinical practise. The medicinal plants: Commiphora mukul and Phyllanthus emblica have considerable DPP-IV inhibitory efficacy, according to our findings. The present study is an extension of the previous study conducted in our laboratory and was designed to confirm the antidiabetic effects of C. mukul and P. emblica in the streptozotocin diabetes model and elucidate the active principles responsible for DPP-IV inhibition. C. mukul (Guggul) and P. emblica (Amla) have the ability to inhibit DPP-IV and have anti-diabetic properties in a Type 2 diabetes mellitus experimental model. The binding sites and affinity of the active principles of C. mukul (Gluggusterone E, Gluggusterone Z) and P. emblica (Pzrogallol, beta-glucogallin, and gallic acid) responsible for DPP-IV enzyme inhibition were identified using in silico studies and compared to Vildagliptin, a synthetic DPP-IV inhibitor. The Vildagliptin and therapy groups had significantly lower glycated hemoglobin and DPP-IV levels. The anti-diabetic effect of C. mukul and P. emblica is due to their DPP-IV inhibitory action. The DPP-IV inhibitory action of Gluggusterone E, Gluggusterone Z, and beta-Glucogallin was found to be superior to Vildagliptin in docking tests.
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spelling pubmed-86417382021-12-14 Antidiabetic activity of Commiphora mukul and Phyllanthus emblica and Computational analysis for the identification of active principles with dipeptidyl peptidase IV inhibitory activity Mohanty, Ipseeta Ray Kumar, C. Selvaa Borde, Manjusha Indian J Pharmacol Short Communication The medicinal plants may serve as natural alternatives to synthetic antidiabetic medications such as dipeptidyl peptidase-IV (DPP-IV) inhibitors, which are commonly prescribed in clinical practise. The medicinal plants: Commiphora mukul and Phyllanthus emblica have considerable DPP-IV inhibitory efficacy, according to our findings. The present study is an extension of the previous study conducted in our laboratory and was designed to confirm the antidiabetic effects of C. mukul and P. emblica in the streptozotocin diabetes model and elucidate the active principles responsible for DPP-IV inhibition. C. mukul (Guggul) and P. emblica (Amla) have the ability to inhibit DPP-IV and have anti-diabetic properties in a Type 2 diabetes mellitus experimental model. The binding sites and affinity of the active principles of C. mukul (Gluggusterone E, Gluggusterone Z) and P. emblica (Pzrogallol, beta-glucogallin, and gallic acid) responsible for DPP-IV enzyme inhibition were identified using in silico studies and compared to Vildagliptin, a synthetic DPP-IV inhibitor. The Vildagliptin and therapy groups had significantly lower glycated hemoglobin and DPP-IV levels. The anti-diabetic effect of C. mukul and P. emblica is due to their DPP-IV inhibitory action. The DPP-IV inhibitory action of Gluggusterone E, Gluggusterone Z, and beta-Glucogallin was found to be superior to Vildagliptin in docking tests. Wolters Kluwer - Medknow 2021 2021-11-24 /pmc/articles/PMC8641738/ /pubmed/34854407 http://dx.doi.org/10.4103/ijp.IJP_69_19 Text en Copyright: © 2021 Indian Journal of Pharmacology https://creativecommons.org/licenses/by-nc-sa/4.0/This is an open access journal, and articles are distributed under the terms of the Creative Commons Attribution-NonCommercial-ShareAlike 4.0 License, which allows others to remix, tweak, and build upon the work non-commercially, as long as appropriate credit is given and the new creations are licensed under the identical terms.
spellingShingle Short Communication
Mohanty, Ipseeta Ray
Kumar, C. Selvaa
Borde, Manjusha
Antidiabetic activity of Commiphora mukul and Phyllanthus emblica and Computational analysis for the identification of active principles with dipeptidyl peptidase IV inhibitory activity
title Antidiabetic activity of Commiphora mukul and Phyllanthus emblica and Computational analysis for the identification of active principles with dipeptidyl peptidase IV inhibitory activity
title_full Antidiabetic activity of Commiphora mukul and Phyllanthus emblica and Computational analysis for the identification of active principles with dipeptidyl peptidase IV inhibitory activity
title_fullStr Antidiabetic activity of Commiphora mukul and Phyllanthus emblica and Computational analysis for the identification of active principles with dipeptidyl peptidase IV inhibitory activity
title_full_unstemmed Antidiabetic activity of Commiphora mukul and Phyllanthus emblica and Computational analysis for the identification of active principles with dipeptidyl peptidase IV inhibitory activity
title_short Antidiabetic activity of Commiphora mukul and Phyllanthus emblica and Computational analysis for the identification of active principles with dipeptidyl peptidase IV inhibitory activity
title_sort antidiabetic activity of commiphora mukul and phyllanthus emblica and computational analysis for the identification of active principles with dipeptidyl peptidase iv inhibitory activity
topic Short Communication
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8641738/
https://www.ncbi.nlm.nih.gov/pubmed/34854407
http://dx.doi.org/10.4103/ijp.IJP_69_19
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