Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1371851 | Bioorganic & Medicinal Chemistry Letters | 2009 | 4 Pages |
Abstract
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-NH2) showed the strongest inhibitory activity, which was maintained for over 3 months at 50 °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.
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Related Topics
Physical Sciences and Engineering
Chemistry
Organic Chemistry
Authors
Jin-Mi Noh, Seon-Yeong Kwak, Hyo-Suk Seo, Joo-Hyun Seo, Byung-Gee Kim, Yoon-Sik Lee,