Structure and inhibition mechanism of some synthetic compounds and phenolic derivatives as tyrosinase inhibitors: review and new insight

AbstractSafety concerns are the primary consideration to identify and detection of enzyme inhibitors. In this regard, safe and potent tyrosinase inhibitors play important role in enhancing nutritional quality, health promotion and also prevent further damages. The present review focuses on the recent and efficient tyrosinase inhibitors discovered from both synthetic sources and synthesized phenolic compounds, including flavonoid, carvacrol, thymol, cinnamic acid and resorcinol derivatives. The inhibitory activity of these compounds was analyzed according to chemical structure, IC50, Ki and their binding energy. Further, inhibition mechanism and the biological effects of some these inhibitors with potential application in food, agricultural, cosmetic and pharmaceutical industries were briefly discussed. Molecular docking procedure was performed on some derivatives and demonstrated favorable binding affinity with amino acid residues of mushroom tyrosinase (PDB ID: 2Y9X). The information offered showed that the substitution pattern of hydroxyl groups at the phenyl ring is an important factor of tyrosinase inhibitory activity. The results confirmed that understanding structural modification of inhibitors is a key role in finding novel and efficacious tyrosinase inhibitors.Communicated by Ramaswamy H. SarmaKeywords: Tyrosinasesynthetic inhibitorsstructuremolecular dockingdrug design Disclosure statementThe author declares no conflict of interest.FundingThe author(s) reported there is no funding associated with the work featured in this article.