Evaluation of in vitro inhibitory effects of some natural compounds on tyrosinase activity and molecular docking study: Antimelanogenesis potential.

Tyrosinase enzyme is a functional oxidase that is extensively divided in nature. It is the main enzyme in melanin synthesis and is also involved in designating the color of mammalian hair and skin. Additionally, it is accountable for the unfavorable enzymatic browning that happens in plant-derived foods, limiting the shelf-life of new-cut crops with the resultant economic harm. Recently, there has been a remarkable concern to study the inhibitory activity of the tyrosinase enzyme and some inhibitory molecules isolated from natural sources. For tyrosinase enzyme, afzelin, narcissoside, justiciresinol, thalassiolin B, carpachromene, neobavaisoflavone, and kojic acid (as standard) as natural phenols have IC50 values in the range of 2.37-7.90 µM. Theoretical methods, such as gaussian software program and molecular modeling, were used to compare the biological and chemical activity values of molecules. To compare the biochemical and chemical activity values of molecules, chemical activities with quantum chemical parameters, and biological activities against tyrosinase with the ID of 5M8L molecules were investigated.