Synthesis, in vitro α-amylase, α-glucosidase activities and molecular docking study of new benzimidazole bearing thiazolidinone derivatives

Abstract

We have synthesized a series of benzimidazole bearing thiazolidinone derivatives (1-20), characterized through NMR and HREI-MS and screened against α-glucosidase and α-amylase activities. All derivatives exhibited varied α-glucosidase inhibitory potential ranging from 1.20 ± 0.10 to 24.60 ± 0.40 μM under the positive control of standard drug acarbose (IC50 = 11.29 ± 0.07 μM); while for α-amylase, inhibitory potential ranging from 1.30 ± 0.10 to 25.70 ± 0.40 μM as compared to standard drug acarbose (IC50 = 11.12 ± 0.15 μM). In both cases; analogue 1 (IC50 values = 1.20 ± 0.10 and 1.30 ± 0.10 µM respectively) and analogue 7 (IC50 values = 2.10 ± 0.10 and 2.7 ± 0.10 µM, respectively) were found with excellent inhibitory potential while remaining analogues of the series showed good to excellent inhibition. Moreover, Structure activity relationship was established and molecular docking study of the most potent analogues was confirmed through binding interaction with the active site of enzymes.