Computational studies on inhibitory effects of Steppogenin against collagenase as an Anti-aging agent
Computational studies on inhibitory effects of Steppogenin against collagenase as an Anti-aging agent
Tanin Kaghazchi,1Fatemeh Sholehvar,2,*
1. Department of Biology, Faculty of Sciences, Zand Institute of Higher Education, Shiraz, Iran 2. Department of Biology, Faculty of Sciences, Zand Institute of Higher Education, Shiraz, Iran
Introduction: Collagenase is a type of matrix metalloproteinase in three forms that digests triple-helical collagen, an essential structural protein in human skin. This collagen degradation is crucial in various activities like breaking down old tissue, building new tissue, and involving specific cells. After biological aging, there is a marked increase in collagenase activity, leading to modifications in collagen configuration within the extracellular matrix, which subsequently results in skin changes such as wrinkles. Flavonoids are polyphonic compounds that are primarily found in fruit and food plants. Flavonoids have significant antioxidant features that help protect the skin from oxidative damage. Steppogenin is classified as a flavonoid and is commonly found in Moraceo plants. This compound's inhibitory features, such as its role in inhibiting tyrosinase, are proven. However, its inhibitory effect on collagenase has not been thoroughly studied. This study aims to investigate the inhibitory effect of steppogenin on collagenase enzymes using computational studies.
Methods: We started the study, by extracting steppogenin from the PubChem site and converting it into a PDB format suitable for the docking process. The collagenase enzyme was obtained from the RCSB PDB site using the 2D1N code, and unnecessary parts of the protein, such as water molecules, were eliminated to get a clearer view of the interactions later in docking. Molecular docking was carried out to investigate the interaction between Steppogenin and collagenase using AutoDock Vina.
Results: Steppogenin and collagenase enzyme (code: 2D1N) formed a ligand-protein complex through hydrogen bonding with an affinity of -8.448 kcal/mol. Two chains A and B are connected to the ligand. ARG155 created the first hydrogen bond in the B chain, where the NH2 group of the protein interacted with the oxygen atom of the ligand. ILE122 formed the second hydrogen bond in the A chain, where the protein's oxygen atom interacted with the ligand's hydrogen atom.
Conclusion: Based on the results of bioinformatic interactions, it is recommended that the inhibitory property of steppogenin be investigated in laboratory conditions.