Key Laboratory of Interfacial Physics and Technology, Shanghai Institute of Applied Physics, Chinese Academy of Sciences , Shanghai , China.
University of Chinese Academy of Sciences , Beijing , China.
J Enzyme Inhib Med Chem. 2019 Dec;34(1):1633-1640. doi: 10.1080/14756366.2019.1661401.
Tyrosinase is a key enzyme involved in melanin synthesis. Therefore, various tyrosinase inhibitors have been screened by researchers in recent years. In the present study, we discovered a novel tyrosinase inhibitor, a peptide ECGYF (named EF-5), with free radical scavenging ability. The effect of tyrosinase inhibition by EF-5 was stronger than that of arbutin and glutathione, when analyzed both (IC50: 0.46 mM) and . The UV-Vis absorption and circular dichroism spectroscopies indicated that EF-5 interacted with tyrosinase in a different way as that of glutathione. The results of molecular docking showed that the binding between EF-5 and tyrosinase was determined majorly by hydrogen bonds and hydrophobic interactions. EF-5 had also retained its ability to scavenge both hydroxyl and superoxide radicals and was found to be nontoxic to cells, as revealed by the MTT assay. These features suggested that the EF-5 peptide may serve as a safe and effective alternative as a tyrosinase inhibitor.
酪氨酸酶是参与黑色素合成的关键酶。因此，近年来研究人员筛选出了各种酪氨酸酶抑制剂。本研究发现了一种新型的酪氨酸酶抑制剂，一种具有自由基清除能力的肽 ECGYF（命名为 EF-5）。当分析其对酪氨酸酶的抑制作用时，EF-5 的效果强于熊果苷和谷胱甘肽（IC50：0.46mM）和 。紫外可见吸收和圆二色性光谱表明，EF-5 与酪氨酸酶的相互作用方式与谷胱甘肽不同。分子对接结果表明，EF-5 与酪氨酸酶的结合主要取决于氢键和疏水相互作用。EF-5 还保留了清除羟基和超氧自由基的能力，并且通过 MTT 测定法发现对细胞无毒。这些特征表明，EF-5 肽可用作安全有效的酪氨酸酶抑制剂替代物。
