feruloyltyramine and kojic-acid

Melanin play a major role in human skin protection and their biosynthesis is vital. Due to their color, they contribute to the skin pigmentation. Tyrosinase is a key enzyme involved in the first stage of melanin synthesis, catalyzing the transformation of tyrosine to l-dopaquinone. The aim of the present study was to study molecules able to inhibit melanin synthesis through inhibition of tyrosinase and their potential use in treating pigmentation-related disorders. We targeted amides obtained from coupling p-hydroxycinnamic acid derivatives with phenylalkylamines. The biological activity was evaluated on human melanocytes by an assay which measures tyrosine-catalyzed L-Dopa oxidation. The most active amides were: trans-N-caffeoyltyramine, N-dihydrocaffeoyltyramine, and trans-N-dihydro-p-hydroxycinnamoyltyramine which induce complete inhibition at 0.1mM. At the latter concentration, kojic acid, which was used as the reference inhibitor, was inactive.

Topics: Amides; Benzoquinones; Caffeic Acids; Catalysis; Cells, Cultured; Dihydroxyphenylalanine; Enzyme Inhibitors; Humans; Levodopa; Melanins; Melanocytes; Monophenol Monooxygenase; Oxidation-Reduction; Pigmentation Disorders; Pyrones; Skin; Structure-Activity Relationship; Tyramine; Tyrosine