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Investigations on Binding Pattern of Kinase Inhibitors with PPARγ: Molecular Docking, Molecular Dynamic Simulations, and Free Energy Calculation Studies
Peroxisome proliferator-activated receptor gamma (PPARγ) is a potential target for the treatment of several disorders. In view of several FDA approved kinase inhibitors, in the current study, we have investigated the interaction of selected kinase inhibitors with PPARγ using computational modeling,...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Hindawi Publishing Corporation
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5340984/ https://www.ncbi.nlm.nih.gov/pubmed/28321247 http://dx.doi.org/10.1155/2017/6397836 |
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author | Mazumder, Mohit Ponnan, Prija Das, Umashankar Gourinath, Samudrala Khan, Haseeb Ahmad Yang, Jian Sakharkar, Meena Kishore |
author_facet | Mazumder, Mohit Ponnan, Prija Das, Umashankar Gourinath, Samudrala Khan, Haseeb Ahmad Yang, Jian Sakharkar, Meena Kishore |
author_sort | Mazumder, Mohit |
collection | PubMed |
description | Peroxisome proliferator-activated receptor gamma (PPARγ) is a potential target for the treatment of several disorders. In view of several FDA approved kinase inhibitors, in the current study, we have investigated the interaction of selected kinase inhibitors with PPARγ using computational modeling, docking, and molecular dynamics simulations (MDS). The docked conformations and MDS studies suggest that the selected KIs interact with PPARγ in the ligand binding domain (LBD) with high positive predictive values. Hence, we have for the first time shown the plausible binding of KIs in the PPARγ ligand binding site. The results obtained from these in silico investigations warrant further evaluation of kinase inhibitors as PPARγ ligands in vitro and in vivo. |
format | Online Article Text |
id | pubmed-5340984 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Hindawi Publishing Corporation |
record_format | MEDLINE/PubMed |
spelling | pubmed-53409842017-03-20 Investigations on Binding Pattern of Kinase Inhibitors with PPARγ: Molecular Docking, Molecular Dynamic Simulations, and Free Energy Calculation Studies Mazumder, Mohit Ponnan, Prija Das, Umashankar Gourinath, Samudrala Khan, Haseeb Ahmad Yang, Jian Sakharkar, Meena Kishore PPAR Res Research Article Peroxisome proliferator-activated receptor gamma (PPARγ) is a potential target for the treatment of several disorders. In view of several FDA approved kinase inhibitors, in the current study, we have investigated the interaction of selected kinase inhibitors with PPARγ using computational modeling, docking, and molecular dynamics simulations (MDS). The docked conformations and MDS studies suggest that the selected KIs interact with PPARγ in the ligand binding domain (LBD) with high positive predictive values. Hence, we have for the first time shown the plausible binding of KIs in the PPARγ ligand binding site. The results obtained from these in silico investigations warrant further evaluation of kinase inhibitors as PPARγ ligands in vitro and in vivo. Hindawi Publishing Corporation 2017 2017-02-22 /pmc/articles/PMC5340984/ /pubmed/28321247 http://dx.doi.org/10.1155/2017/6397836 Text en Copyright © 2017 Mohit Mazumder et al. https://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Article Mazumder, Mohit Ponnan, Prija Das, Umashankar Gourinath, Samudrala Khan, Haseeb Ahmad Yang, Jian Sakharkar, Meena Kishore Investigations on Binding Pattern of Kinase Inhibitors with PPARγ: Molecular Docking, Molecular Dynamic Simulations, and Free Energy Calculation Studies |
title | Investigations on Binding Pattern of Kinase Inhibitors with PPARγ: Molecular Docking, Molecular Dynamic Simulations, and Free Energy Calculation Studies |
title_full | Investigations on Binding Pattern of Kinase Inhibitors with PPARγ: Molecular Docking, Molecular Dynamic Simulations, and Free Energy Calculation Studies |
title_fullStr | Investigations on Binding Pattern of Kinase Inhibitors with PPARγ: Molecular Docking, Molecular Dynamic Simulations, and Free Energy Calculation Studies |
title_full_unstemmed | Investigations on Binding Pattern of Kinase Inhibitors with PPARγ: Molecular Docking, Molecular Dynamic Simulations, and Free Energy Calculation Studies |
title_short | Investigations on Binding Pattern of Kinase Inhibitors with PPARγ: Molecular Docking, Molecular Dynamic Simulations, and Free Energy Calculation Studies |
title_sort | investigations on binding pattern of kinase inhibitors with pparγ: molecular docking, molecular dynamic simulations, and free energy calculation studies |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5340984/ https://www.ncbi.nlm.nih.gov/pubmed/28321247 http://dx.doi.org/10.1155/2017/6397836 |
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