Abstract
Tyrosinase is a key enzyme in melanogenesis, playing an important role in skin, hair, and eye pigmentation, as well as in the enzymatic browning of fruits and vegetables. Excessive tyrosinase activity leads to hyperpigmentation and other dermatological problems, and it also causes losses in the food industry. For this reason, tyrosinase inhibitors have become the subject of intensive research in medicine, cosmetology, and food technology. Among various inhibitors, compounds containing ketone and hydroxyl groups draw special attention, because they have the ability to chelate copper ions in enzyme's active center or block access to it. This article discusses the possible mechanisms of action, based on molecular modeling of interaction of PDB database retrieved model of enzyme with known natural inhibitors-kojic acid and tropolone, as well as 6-hydroxyimino derivatives of imidazo[1,2-a]imidazole-5-ones. The results suggest that the model of enzyme-ligand interaction can be useful in establishing affinity to tyrosinase of new natural and synthetic inhibitors, which can have broad applications in various fields, particularly in medicine and cosmetology, with promising prospects for further development.