Noh Jin-Mi, Kwak Seon-Yeong, Seo Hyo-Suk, Seo Joo-Hyun, Kim Byung-Gee, Lee Yoon-Sik
School of Chemical and Biological Engineering, Seoul National University, Seoul 151-744, Republic of Korea.
Bioorg Med Chem Lett. 2009 Oct 1;19(19):5586-9. doi: 10.1016/j.bmcl.2009.08.041. Epub 2009 Aug 14.
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.
曲酸（KA）是一种著名的酪氨酸酶抑制剂，但其抑制活性和稳定性不足。我们用氨基酸对曲酸进行了修饰，并筛选了它们对酪氨酸酶的抑制活性。其中，曲酸-苯丙氨酸酰胺（KA-F-NH₂）表现出最强的抑制活性，在50℃下可保持3个月以上，动力学分析表明其为非竞争性抑制剂。它还表现出多巴色素还原活性。我们还根据对接模拟数据提出了一种新的酪氨酸酶抑制机制。
