Picolyl alkyl amines as novel tyrosinase inhibitors: Influence of hydrophobicity and substitution

Article abstract of DOI:10.1021/jf902100k

Several novel picolyl alkyl amine derivatives (A-L) were synthesized, and the influence of hydrophobicity and substitution on the inhibition of mushroom tyrosinase toward both monophenolase and dlphenolase activities are described, α-, β-, and γ-picolyl amines are neither the substrates nor the inhibitors; however, the inhibition Is induced by the incorporation of an alkyl chain. The inhibition was strongly dependent on the substitution on a pyridine ring, and the inhibition follows the trend of a-picolyl alkyl amines (A, D, G) < β-picolyl alkyl amines (B, E, H) < γ -picolyl alkyl amines (C, F, I). The inhibition kinetics have been investigated, and γ-substituted derivatives were found to be a mixed type of inhibitor, whereas β-substituted derivatives were found to exhibit uncompetitive inhibition toward the oxidation of L-DOPA.