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 analysis which was further validated by 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 IC values, 47.93 ± 5.21 and 45.86 ± 3.78 , respectively, showed weaker effect than acarbose (4.6 ± 1.26 ) on α-amylase but showed significant effect to inhibit α-glucosidase (32.23 ± .556 and 31.26 ± .556 , respectively). IC value of resveratrol and taxifolin (5.638 ± .0016 and 6.691 ± .004 ) in comparison to diprotin A (IC: 7.21 ± .021 ) 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 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.