Department of Physics, University of Calabria , Ponte P. Bucci, Cubo 31C, 87036 Rende (CS), Italy.
J Agric Food Chem. 2014 May 14;62(19):4384-91. doi: 10.1021/jf405584a. Epub 2014 May 5.
Spectrophotometry and fluorescence combined with docking and molecular dynamics simulations are used to study the effect of the carrier proteins β-lactoglobulin and human serum albumin on the degradative trans-to-cis conversion of resveratrol. The spectroscopic measurements quantify the concentration of resveratrol isoforms after 2 h of irradiation with light at 340 nm, showing that their ratio depends linearly on temperature between 20 and 50 °C and obeys an Arrhenius law with activation energies of photoisomerization of 7.8 and 11.2 kcal/mol for β-lactoglobulin and albumin, respectively, compared to 5.1 kcal/mol in solution. Thus, both proteins protect trans-resveratrol from degradation, with albumin being more effective than β-lactoglobulin. The computational techniques clarify details of the binding of trans-resveratrol to the proteins and show that the stabilizing effect correlates with an increase of the dihedral order parameter of the ligand. These findings suggest that transport proteins are viable carriers to stabilize and deliver resveratrol in vivo in the biologically effective trans form.
分光光度法和荧光法结合对接和分子动力学模拟，用于研究载体蛋白β-乳球蛋白和人血清白蛋白对白藜芦醇的降解反式-顺式转化的影响。光谱测量定量了在 340nm 光照射 2 小时后白藜芦醇异构体的浓度，结果表明它们的比例随温度在 20 到 50°C 之间呈线性变化，并遵循阿伦尼乌斯定律，β-乳球蛋白和白蛋白的光异构化的活化能分别为 7.8 和 11.2 kcal/mol，而在溶液中为 5.1 kcal/mol。因此，两种蛋白质都能保护反式白藜芦醇免受降解，白蛋白比β-乳球蛋白更有效。计算技术阐明了反式白藜芦醇与蛋白质结合的细节，并表明稳定作用与配体的二面角有序参数的增加相关。这些发现表明，转运蛋白是一种可行的载体，可以在体内以生物有效形式稳定和输送反式白藜芦醇。
