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

Abstract

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 [Formula: see text] and 45.86 ± 3.78 [Formula: see text], respectively, showed weaker effect than acarbose (4.6 ± 1.26 [Formula: see text]) on α-amylase but showed significant effect to inhibit α-glucosidase (32.23 ± .556 [Formula: see text] and 31.26 ± .556 [Formula: see text], respectively). IC50 value of resveratrol and taxifolin (5.638 ± .0016 [Formula: see text] and 6.691 ± .004 [Formula: see text]) in comparison to diprotin A (IC50: 7.21 ± .021 [Formula: see text]) 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.