Kojic acid-amino acid conjugates as tyrosinase inhibitors.
Kojic acid (KA), a well known tyrosinase inhibitor, has insufficient inhibitory activity and stability. We modified KA with amino acids and screened their tyrosinase inhibitory activity. Among them, kojic acid-phenylalanine amide (KA-F-NH(2)) showed the strongest inhibitory activity, which was maintained for over 3 months at 50 degrees C, and acted as a noncompetitive inhibitor as determined by kinetic analysis. It also exhibited dopachrome reducing activity. We also propose a new tyrosinase inhibition mechanism based on the docking simulation data.
Noh
Jin-Mi
JM
School of Chemical and Biological Engineering, Seoul National University, Seoul 151-744, Republic of Korea.
Kwak
Seon-Yeong
SY
Seo
Hyo-Suk
HS
Seo
Joo-Hyun
JH
Kim
Byung-Gee
BG
Lee
Yoon-Sik
YS
D000596:Amino Acids / Q000737:chemistry*; D003198:Computer Simulation; D004791:Enzyme Inhibitors / Q000737:chemistry* / Q000494:pharmacology; D007700:Kinetics; D014442:Monophenol Monooxygenase / Q000037:antagonists & inhibitors* / Q000378:metabolism; D011753:Pyrones / Q000737:chemistry*
D000596:Amino Acids; D004791:Enzyme Inhibitors; D011753:Pyrones; C011890:kojic acid; D014442:Monophenol Monooxygenase