Biochemical Investigation of Inhibitory Activities of Plant-Derived Bioactive Compounds Against Carbohydrate and Glucagon-Like Peptide-1 Metabolizing Enzymes

The aim of current study was to investigate the inhibitory activities of resveratrol and taxifolin against α-amylase, α-glucosidase, and DPP-IV enzymes via in vitro analysis which was further validated by in silico studies. The analysis of molecular docking was also done to determine the binding capabilities of resveratrol and taxifolin with α-amylase, α-glucosidase, and DPP-IV enzymes. Resveratrol and taxifolin having IC50 values, 47.93 ± 5.21 μ M and 45.86 ± 3.78 μ M , respectively, showed weaker effect than acarbose (4.6 ± 1.26 μ M ) on α-amylase but showed significant effect to inhibit α-glucosidase (32.23 ± .556 μ M and 31.26 ± .556 μ M , respectively). IC50 value of resveratrol and taxifolin (5.638 ± .0016 μ M and 6.691 ± .004 μ M ) in comparison to diprotin A (IC50: 7.21 ± .021 μ M ) showed that they have significant inhibitory effect on DPP-IV enzyme. Our results illustrated that resveratrol and taxifolin have potential to prevent the metabolism of carbohydrates via inhibition of α-amylase and α-glucosidase, and prolongs metabolic function of incretin by inhibiting the enzymatic activity of DPP-IV. The results of molecular docking have also revealed that resveratrol and taxifolin have significant affinity to bind with α-amylase, α-glucosidase, and DPP-IV in comparison with standard drugs such as acarbose, miglitol, and diprotin.