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

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 outside the body must suppress this enzyme's growth rate. Several previous studies have stated that Piper betle L. has high antioxidants and inhibits enzyme activity, including allypyrocatechol.Objectives: The current study aimed to evaluate the molecular mechanism of allylpyrocatecachol with SOD, CAT, and GSHPx and determine the lead compounds' potential against some antioxidant enzymes by an in silico approach.Methods: Allylpyrocatechol was docked to SOD, CAT, and GSHPx enzyme using Autodock4 tools. An evaluation of receptor-ligand interactions was conducted based on comparing binding affinity, the accuracy of involved amino acid residues, and 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, and -4.5 kcal/mol for the SOD, CAT, and GHSPx receptors, respectively.Conclusion: This finding indicates that Allylpyrocatechol has a promising candidate as a compound to inhibit antioxidant enzyme activity. It can be seen from the accuracy of the amino acids residue involved and the value of the binding affinity compared to the positive control ligand.