Brayan Roulier, Basile Pérès, Romain Haudecoeur
Journal: Journal of medicinal chemistry 2020;63(22):13428-13443
PMID: 32787103
Human tyrosinase (TYR) is the key enzyme ensuring the conversion of l-tyrosine to dopaquinone, thereby initiating melanin synthesis, i.e., melanogenesis. Although the protein has long been familiar, knowledge about its three-dimensional structure and efficient overexpression protocols emerged only recently. Consequently, for decades medicinal chemistry studies aiming at developing skin depigmenting agents relied almost exclusively on biological assays performed using mushroom tyrosinase (TYR), producing a plethoric literature, often of little useful purpose. Indeed, several recent reports have pointed out spectacular differences in terms of interaction patterns and inhibition values between TYR and TYR, including for widely used standard tyrosinase inhibitors. In this review, we summarize the last developments regarding the potential role of TYR in human pathologies, the advances in recombinant expression systems and structural data retrieving, and the pioneer generation of true TYR inhibitors. Finally, we present suggestions for the design of future inhibitors of this highly attractive target in pharmacology and dermocosmetics.
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