Inhibition of Tyrosinase Activity by N,N-Unsubstituted Selenourea Derivatives

• Published in: Biological & Pharmaceutical Bulletin Vol. 28; no. 5; pp. 838 - 840
• Main Authors: Ha, Sang Keun, Koketsu, Mamoru, Lee, Kunho, Choi, Sang Yoon, Park, Ji-Ho, Ishihara, Hideharu, Kim, Sun Yeou
• Format: Journal Article
• Language: English; Japanese
• Published: Japan The Pharmaceutical Society of Japan 01.05.2005; Pharmaceutical Society of Japan; Japan Science and Technology Agency
• Subjects: Cell Line; Dose-Response Relationship, Drug; Enzyme Activation - drug effects; Enzyme Activation - physiology; Enzyme Inhibitors - pharmacology; Humans; Monophenol Monooxygenase - antagonists & inhibitors; Monophenol Monooxygenase - metabolism; N,N-unsubstituted selenourea; Organoselenium Compounds - chemistry; Organoselenium Compounds - pharmacology; tyrosinase inhibitor; Urea - analogs & derivatives; Urea - chemistry; Urea - pharmacology
• ISSN: 0918-6158; 1347-5215
• DOI: 10.1248/bpb.28.838

This study investigated inhibitory effects of N,N-unsubstituted selenourea derivatives on tyrosinase activity. Three types of N,N-unsubstituted selenoureas derivatives exhibited inhibitory effect on dopa (3,4-dihydroxyphenylalanine) oxidase activity of mushroom tyrosinase. Compound D at a concentration of 200 μM exhibited 55.5% of inhibition on dopa oxidase activity of mushroom tyrosinase. This inhibitory effect was higher than that of kojic acid (39.4%), a well known tyrosinase inhibitor. Moreover, the compound D identified as a noncompetitive inhibitor by Lineweaver–Burk plot analysis. In addition, compound D also inhibited the melanin production in melan-a cells.