Picolyl Alkyl Amines As Novel Tyrosinase Inhibitors: Influence of Hydrophobicity and Substitution

• Published in: Journal of agricultural and food chemistry 2009-10, Vol.57 (20), p.9780-9786
• Main Authors: Bandyopadhyay, Punam, Jha, Sujeetkumar, Imran Ali, S. K
• Format: Article
• Language: English
• Subjects: Agaricales - enzymology; amines; Amines - chemical synthesis; Amines - chemistry; Amines - pharmacology; Biological and medical sciences; catechol oxidase; chemical structure; enzymatic browning; enzyme activity; enzyme inhibition; enzyme inhibitors; Enzyme Inhibitors - chemical synthesis; Enzyme Inhibitors - chemistry; Enzyme Inhibitors - pharmacology; enzyme substrates; food additives; Food Chemistry/Biochemistry; Food industries; Fruit and vegetable industries; Fundamental and applied biological sciences. Psychology; Fungal Proteins - antagonists & inhibitors; Hydrophobic and Hydrophilic Interactions; hydrophobicity; Kinetics; L-dopa; Monophenol Monooxygenase - antagonists & inhibitors; reaction kinetics; structure-activity relationships; synthesis
• ISSN: 0021-8561; 1520-5118
• 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 diphenolase 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 α-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.