Computational Studies of Allylpyrocatechol from Piper betle L. as Inhibitor against Superoxide dismutase, Catalase, and Glutathione peroxidase as Antioxidant Enzyme

Abstract

Background: The most significant antioxidant enzymes are glutathione peroxidase (GSHPx), catalase (CAT), and superoxide dismutase (SOD) have a significant role in the scavenging of free radicals but overexpressing of these enzymes can have deleterious effects. Therefore, compounds from outside the body are needed that can suppress the growth rate of this enzyme. Several previous studies have stated that Piper betle L. has high antioxidant and inhibits enzyme activity including of allypyrocatechol. Objectives: The current study aimed to evaluate the molecular mechanism of allylpyrocatecachol with SOD, CAT, GSHPx and find out its potential of the lead compounds against some antioxidant enzyme by an in silico approach. Methods: Allylpyrocatechol were docked to SOD, CAT, and GSHPx enzyme using Autodock4 tools. Evaluation of receptor-ligand interactions based on comparison of binding affinity, accuracy of involved amino acid residues, and compare with gallic acid as a positive control ligand. Results: By in silico analysis showed that the binding affinity between the ligand and the three receptors were -4.3, -6.8, -4.5 kcal/mol for the SOD, CAT, and GHSPx receptors, respectively. Conclusion: This finding indicates that Allylpyrocatechol have a promising candidate as a compound to inhibits antioxidant enzyme activity. It can be seen from the accuracy of the amino acids residue involved and value of the binding affinity compared to positive control ligand