Synthesis, in vitroα-glucosidase, α-amylase activities and molecular docking study of hybrid thiazole-sulfonohydrazide analogues

Thiazole-sulfonohydrazide hybrid analogues (1–15), were synthesized and characterized through different techniques such as NMR, HR-EIMS and evaluated against α-glucosidase and α-amylase enzymes. In case of α-glucosidase,analogues 4(IC50 = 4.60 ± 0.30 µM) while in case of α-amylase, analogue 1(IC50 = 5.10 ± 0.20 µM) is the most potent among the series confirmed from both the experimental and molecular docking study. Structure activity relationship was carried out for all analogues which mainly depend upon number, nature, position, and electron donating/withdrawing effects of the substituent/s on phenyl ring. Molecular docking study was carried out to show the binding interaction of the most potent analogue with the active site of enzyme.