Investigations on Binding Pattern of Kinase Inhibitors with PPAR γ: Molecular Docking, Molecular Dynamic Simulations, and Free Energy Calculation Studies.

Investigations on Binding Pattern of Kinase Inhibitors with PPARγ: Molecular Docking, Molecular Dynamic Simulations, and Free Energy Calculation Studies.
PPAR Res. 2017;2017:6397836
Authors: Mazumder M, Ponnan P, Das U, Gourinath S, Khan HA, Yang J, Sakharkar MK
Abstract
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.
PMID: 28321247 [PubMed - in process]

Source: PPAR Research - March 24, 2017 Category: Genetics & Stem Cells Tags: PPAR Res Source Type: research