标题：Insights in Binding Mechanism Of Benzofuran Salicylic Acid Inhibitors against Mycobacterium Protein Tyrosine Phosphatases (PTP1B) using Molecular Modelling and Simulation Approaches
期刊名称：International Journal of Innovative Research in Computer and Communication Engineering
印刷版ISSN：2320-9798
电子版ISSN：2320-9801
出版年度：2015
卷号：3
期号：11
DOI：10.15680/IJIRCCE.2015.0311227
出版社：S&S Publications
摘要：The protein tyrosine phosphatase 1B (PTP1B) being virulent phosphatase secreted by Mycobacteriumtuberculosis, which is essential for the survival and persistence of the bacterium in the host and is proposed as a promisingdrug target against tuberculosis infection. Here in silico docking studies of series of benzofuran salicylic acid derivatives asinhibitors for PTP1B were performed. Based on interactions with proximal domain, three compounds were selected as thebest. Molecular Dynamics Simulation study was carried out for these PTP1B docked complexes for better understanding ofbinding mode, binding free energy and stability. MGBSA calculation showed that binding free energy in terms of enthalpyof top three PTP1B complexes were well correlated with experimental IC50 and molecular determinants in binding werealso identified. Based on binding free energy (ΔG), compound 4g (6-hydroxy - 2-phenyl -3-{2-[3- ( trifluoromethyl )phenyl]ethynyl}-1- benzofuran -5-carboxylic acid ) which has more favorable binding free energy compared to othercompounds and hence can be chosen as a potent inhibitor against tuberculosis.
