Study on the Interaction Between 2'-OH-BDE-68 and HAS by Molecular Fluorospectrometry and Molecular Dynamics Simulation

A study on the interaction of 2'-hydroxy-2,3',4,5-tetrabromo diphenyl ethers (2'-OH-BDE-68) with human serum albumin (HSA) and its effect on the conformation of HSA was made by molecular fluorospectrometry, molecular docking and molecular dynamics simulation, under physiological condition of pH 7.4. The results showed as follows:① quenching of the intra-originated fluorescence of HSA by the presence of 2'-OH-BDE-68 was a static process with non-radiative energy transfer. ② The hydrophobic action together with the weak electrostatic effort was the main power for impetus of the interaction, which was proved to be a spontaneous reaction. ③ The interaction of 2'-OH-BDE-68 with HSA attained to equilibrium within 10 ns, and the binding site of the complex was located at Site Ⅰ. ④ That formation of the complex led to enhancement of hydrophobicity of the tryptophan in HSA. As a result of these actions, the secondary conformation of HSA was changed.