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RBMS-01, a quinoline derivative is a novel dipeptidyl peptidase (DPP4) inhibitor was reported. We have identified this DPP-IV inhibitor in silico as an anti-diabetic agent, the mechanism reveals that the quinoline derivative increases the DPP4 function by degrading GLP-1 activity. Further, the study revealed by replacing the quinoline substitution on the various compounds in a more polar group, these compound shows not only enhancing the binding and functional activity of DPP4, also significantly shows the hERG inhibitory activities. Here, it reveals that the library of compounds constructed based on heterocyclic ring and performed docking using GLIDE, in an order with inhibition scores and compared with already existing drugs. An active site of these compounds was determined termed as the lead molecule, the molecule formula is, 6,7,8,9-Tetrahydro-2H-11-oxa- 2,4,10-triaza-benzo(b)fluoren-1-one, (RBMS-01) emerged as a potent, DPP4 inhibitor that displayed. The pharmacophoric analysis also shows that the novel inhibitor have better activity than the other inhibitors.

chemical science transactions

Identification and Comparative Molecular Docking Analysis of 6, 7, 8, 9-Tetrahydro-2H-11-oxa-2, 4, 10-triaza-benzo[B] fluoren-1-one (RBMS-01) Bounds with DPP4 for Anti-Hyperglycemic Activities