Protein-Tyrosine Phosphatase-1B (PTP-1B) Inhibitory Perspectives of Hydroxylated Chalcones: Exploration through Docking Studies

SANTOSH S CHHAJED; NEHA A SALUNKE; Animeshchandra G M Haldar; Kanhaiya M Dadure; DEBARSHI KAR MAHAPATRA

doi:10.37591/(rrjobi).v6i1.307

Abstract

The current research emphasized on exploring the Protein-Tyrosine Phosphatase-1 B (PTP-1B) inhibitory potentials of hydroxylated chalcone derivatives against PDB ID: 4I8N (PTP-1B in complex with an inhibitor [(4-{(2s)-2-(1,3-benzoxazol-2-yl)-2-[(4-fluorophenyl)sulfamoyl]ethyl}phenyl)amino](oxo)acetic acid) by molecular docking approach using the iGEMDOCK (Genetic Evolutionary Method for Molecular Docking) software. The current molecular docking analysis of some hydroxylated chalcone derivatives have presented a profound inhibition of the antidiabetic target PTP-1B by interacting with the amino acid residues such as TYR46, ASP48, ASP181, ASP182, GLY200, CYS215, SER216, ALA217, ARG221, and GLN262 through hydrogen bonding. The hydroxyl group at 3- and 4-positions of A-ring and several electron-donating and electron-withdrawing groups at B-ring of the benzylideneacetophenone scaffold have been seen to exert an enormous role in inhibiting the phosphorylating enzyme. The complete inhibition of this new biological target by low-molecular-weight ligand will open new avenues of modern diabetic therapeutics and will motivate the present-day researchers in emerging pharmacological research. Keywords: Chalcone, PTP-1B, diabetes, hypoglycemic, dockingCite this ArticleSantosh S. Chhajed, Neha A. Salunke, Animeshchandra G.M. Haldar, Kanhaiya M. Dadure, Debarshi Kar Mahapatra. Protein-Tyrosine Phosphatase-1B (PTP-1B) Inhibitory Perspectives of Hydroxylated Chalcones: Exploration through Docking Studies. Research & Reviews: A Journal of Bioinformatics. 2019; 6(1): 4–8p.