2'-羟基-2;4-二溴二苯醚与人血清白蛋白作用机制的光谱研究与计算模拟

Abstract

The interaction between 2'-hydroxy-2,4-dibromo diphenyl ethers (2'-OH-BDE-7) and human serum albumin (HSA) was investigated with molecular docking, molecular dynamics simulation and spectroscopy techniques. The results of synchronous fluorescence spectroscopy indicated that the conformation of HSA was changed when 2'-OH-BDE-7 binding to HSA, which consistent with the results of molecular dynamics simulations. In addition, the results of fluorescence spectroscopy experiment showed that the intrinsic fluorescence quenching of HSA was reduced by 2'-OOH-BDE-7. Static quenching and non-radiation energy transfer are the two main reasons leading to the fluorescence quenching of HSA by 2'-OH-BDE-7. In the process of binding, the entropy, the enthalpy and the Gibbs free energy were negative, which suggested that the interaction between 2'-OH-BDE-7 and HSA was driven mainly by hydrophobic forces and van de Waals forces. Finally, a similar conclusion was obtained from the competitive experiment and molecular docking, which shown 2'-OH-BDE-7 binded human serum albumin at site I. Excellent agreement was founded between computer simulations results and spectral experiments to provide more information for the mechanism study on the interaction between 2'-OH-BDE-7 and HSA.