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Coumarin-Based Sulfonamide Derivatives As Potential DPP-IV Inhibitors

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dc.contributor.author Vawhal, Pallavi Kishor
dc.contributor.author Jadhav, Shailaja B.
dc.contributor.author Kaushik, Sumit
dc.contributor.author Panigrahi, Kahnu Charan
dc.contributor.author Nayak, Chandan
dc.contributor.author Urmee, Humaira
dc.contributor.author Khan, Sharuk L.
dc.contributor.author Siddiqui, Falak A.
dc.contributor.author Islam, Fahadul
dc.contributor.author Eftekhari, Aziz
dc.contributor.author Alzahrani, Abdullah R.
dc.contributor.author Azlina, Mohd Fahami Nur
dc.contributor.author Sarker, Md. Moklesur Rahman
dc.contributor.author Ibrahim, Ibrahim Abdel Aziz
dc.date.accessioned 2024-05-08T09:08:43Z
dc.date.available 2024-05-08T09:08:43Z
dc.date.issued 2023-01-19
dc.identifier.issn 1420-3049
dc.identifier.uri http://dspace.daffodilvarsity.edu.bd:8080/handle/123456789/12299
dc.description.abstract Recent research on dipeptidyl peptidase-IV (DPP-IV) inhibitors has made it feasible to treat type 2 diabetes mellitus (T2DM) with minimal side effects. Therefore, in the present investigation, we aimed to discover and develop some coumarin-based sulphonamides as potential DPP-IV inhibitors in light of the fact that molecular hybridization of many bioactive pharmacophores frequently results in synergistic activity. Each of the proposed derivatives was subjected to an in silico virtual screening, and those that met all of the criteria and had a higher binding affinity with the DPP-IV enzyme were then subjected to wet lab synthesis, followed by an in vitro biological evaluation. The results of the pre-ADME and pre-tox predictions indicated that compounds 6e, 6f, 6h, and 6m to 6q were inferior and violated the most drug-like criteria. It was observed that 6a, 6b, 6c, 6d, 6i, 6j, 6r, 6s, and 6t displayed less binding free energy (PDB ID: 5Y7H) than the reference inhibitor and demonstrated drug-likeness properties, hence being selected for wet lab synthesis and the structures being confirmed by spectral analysis. In the in vitro enzyme assay, the standard drug Sitagliptin had an IC50 of 0.018 µM in the experiment which is the most potent. All the tested compounds also displayed significant inhibition of the DPP-IV enzyme, but 6i and 6j demonstrated 10.98 and 10.14 µM IC50 values, respectively, i.e., the most potent among the synthesized compounds. Based on our findings, we concluded that coumarin-based sulphonamide derivatives have significant DPP-IV binding ability and exhibit optimal enzyme inhibition in an in vitro enzyme assay. en_US
dc.language.iso en_US en_US
dc.publisher MDPI Publications en_US
dc.subject Computational analysis en_US
dc.subject Hypoglycemia en_US
dc.title Coumarin-Based Sulfonamide Derivatives As Potential DPP-IV Inhibitors en_US
dc.title.alternative Pre-ADME Analysis, Toxicity Profile, Computational Analysis, and In Vitro Enzyme Assay en_US
dc.type Article en_US


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