Synthesis, X-ray diffraction analysis, quantum chemical studies and α-amylase inhibition of probenecid derived S-alkylphthalimide-oxadiazole-benzenesulfonamide hybrids. (31st December 2022)

• Record Type: Journal Article
• Authors: Khan, Bilal Ahmad; Hamdani, Syeda Shamila; Ahmed, Muhammad Naeem; Hameed, Shahid; Ashfaq, Muhammad; Shawky, Ahmed M.; Ibrahim, Mahmoud A. A.; Sidhom, Peter A.
• Is Part Of: Journal of enzyme inhibition and medicinal chemistry. Volume 37:Number 1(2022)
• Page Start: 1464
• Page End: 1478
• Publication Date: 2022-12-31
• Subjects: Oxadiazole -- probenecid -- X-ray diffraction -- enzyme inhibition -- molecular modelling; Enzyme inhibitors -- Periodicals; Enzyme Inhibitors -- periodicals; Biochemistry -- periodicals; 572.7
• DOI: 10.1080/14756366.2022.2078969
• Languages: English
• ISSNs: 1475-6366

Abstract

Abstract: Sulphonamide and 1, 3, 4-oxadiazole moieties are present as integral structural parts of many drugs and pharmaceuticals. Taking into account the significance of these moieties, we herein present the synthesis, single-crystal X-ray analysis, DFT studies, and α -amylase inhibition of probenecid derived two S -alkylphthalimide-oxadiazole-benzenesulfonamide hybrids. The synthesis has been accomplished in high yields. The final structures of both hybrids have been established completely with the help of different spectro-analytical techniques, including NMR, FTIR, HR-MS, and single-crystal X-ray diffraction analyses. In an effort to confirm the experimental findings, versatile quantum mechanical calculations and Hirshfeld Surface analysis have been performed. α -Amylase inhibition assay has been executed to investigate the enzyme inhibitory potential of both hybrids. The low IC50 value (76.92 ± 0.19 μg/mL) of hybrid 2 shows the good α -amylase inhibition potential of the respective compound. Ultimately, the binding affinities and features of the two hybrids are elucidated utilising a molecular docking technique against the α -amylase enzyme.