Journal article Open Access

DESIGN & MOLECULAR DOCKING STUDIES OF COUMARIN SUBSTITUTED 1, 3, 4-OXADIAZOLES AS GLYCOGEN SYNTHASE KINASE-3 INHIBITORS.

Purohit S.S.*, Kulkarni V.H., Joshi S.D.

Glycogen synthase kinase 3 (GSK-3) is a serine/threonine protein kinase that mediates the addition of phosphate molecules onto serine and threonine amino acid residues. First discovered in 1980 as a regulatory kinase for its namesake, Glycogen synthase, GSK-3 has since been identified as a kinase for over forty different proteins in a variety of different pathways. GSK-3 has recently been the subject of much research because it has been implicated in a number of diseases, including Type II diabetes (Diabetes mellitus type 2), Alzheimer's Disease, inflammation, cancer, and bipolar disorder. A plethora of GSK-3 inhibitors has been described and most of the effects were observed in vitro and cellular studies. Present study is aimed at design of GSK-3 Inhibitors, their molecular docking studies using online molecular docking software, i.e. www. Dockingserver.com. Based upon previous studies on 1, 3, 4-oxadiazoles as GSK-3 inhibitors, 1, 3, 4-oxadiazole molecule skeleton was taken as the core skeleton & 4 different modifications were made. The compounds were docked with GSK (PDB ID: 3f88 and PDB ID: 4E7W).The results have shown appreciable molecular docking interactions with the GSK-3 protein amino acid residues. The Est. inhibition constant, Ki values for the ligands were observed in µM values. . It is observed that Ligand I has shown Est. free energy of binding -10.17 which is said to be better than the other 3 ligands & reference ligands.

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