Hridya Hemachandran, Amrita Anantharaman, Sankari Mohan, George Priya Doss C, Gopalakrishnan Mohan, Gopalakrishnan Chandrasekaran, Siva Ramamoorthy
School of Bio Sciences and Technology, VIT University, Vellore 632014, Tamil Nadu, India.
School of Advanced Sciences, VIT University, Vellore 632014, Tamil Nadu, India.
Int J Biol Macromol. 2015 Nov;81:228-34. doi: 10.1016/j.ijbiomac.2015.07.064. Epub 2015 Aug 5.
In our present study, the inhibitory effect of brazilein from Caesalpinia sappan on tyrosinase activity was investigated through multi-spectroscopic and molecular docking techniques. The result has shown that brazilein reversibly inhibited tyrosinase in a mixed type manner. The interaction of brazilein with the amino acid residues of tyrosinase has been validated through fluorescence quenching studies. Copper interaction studies suggested that brazilein could bind with copper ions of the enzyme. Circular dichroism analysis confirmed that brazilein induced secondary structural changes in tyrosinase. Docking studies further authenticate that brazilein forms hydrophobic and hydrogen bonding with the active site residues of tyrosinase. Moreover, in vitro studies confirmed that the inhibitory mechanism of cellular tyrosinase and melanin synthesis by brazilein in B16F0 melanoma cells. These results suggested that brazilein act as a potential tyrosinase inhibitor and it would contribute as a of novel tyrosinase inhibitor in food, cosmetic and pharmaceutical industry.
在我们目前的研究中，通过多光谱和分子对接技术研究了苏木中巴西苏木素对酪氨酸酶活性的抑制作用。结果表明，巴西苏木素以混合型方式可逆地抑制酪氨酸酶。通过荧光猝灭研究验证了巴西苏木素与酪氨酸酶氨基酸残基的相互作用。铜相互作用研究表明，巴西苏木素可与该酶的铜离子结合。圆二色性分析证实，巴西苏木素诱导了酪氨酸酶二级结构的变化。对接研究进一步证实，巴西苏木素与酪氨酸酶的活性位点残基形成疏水和氢键。此外，体外研究证实了巴西苏木素对B16F0黑色素瘤细胞中细胞酪氨酸酶和黑色素合成的抑制机制。这些结果表明，巴西苏木素可作为一种潜在的酪氨酸酶抑制剂，并将在食品、化妆品和制药行业中作为新型酪氨酸酶抑制剂发挥作用。
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