Abstract：Hexabromocyclododecane (HBCD) is widely used in industry as a kind of brominated flame retardant. However, more and more people pay close attention to the problem of HBCD contamination in the environment due to its potential risk to human health. There are no reports focuses on the transport mechanism of HBCD in the human body. Hence, multi-spectroscopy and computer simulation methods investigated the interaction mechanisms of HBCD and bovine serum albumin (BSA)-. The solution experiments confirmed that HBCD quenched BSA’s intrinsic fluorescence through the static quench mechanism and non-radiation energy transfer. The binding constants (Ka) between them were 2.796 6×104 L·mol-1 (288 K), 2.194 1×104 L·mol-1 (293 K), and 1.174 4×104 L·mol-1 (298 K), respectively. The number of the binding site in the BSA-HBCD complex was approximately equal to 1. The thermodynamic constants were calculated to be ΔH=-61.749 kJ·mol-1 and ΔS=-128.742 J·(mol·K)-1, indicating that van der Waals or hydrogen bond play a key role in this binding process. The result of molecular docking and fluorescence spectrum indicated that the primary binding site for HBCD was located in the hydrophobic pocket of sub-domain Ⅱ A of BSA, and the binding distance was about 3.45 nm. The secondary conformation of BSA did not affect by HBCD was observed in three-dimensional fluorescence spectra and MD simulations. This research provides a theoretical basis for further understanding of toxic effects of HBCD on human toxicity.
Key words：Hexabromocyclododecane; Multi-spectroscopy; Computer Simulation; Bovine serum albumin
庹 浔，宋继敏，付 豪，吕小兰. 光谱法与计算机模拟法研究六溴环十二烷与牛血清白蛋白的相互作用[J]. 光谱学与光谱分析, 2021, 41(05): 1487-1492.
TUO Xun, SONG Ji-min, FU Hao, LÜ Xiao-lan. Study on Interaction Between Hexabromocyclododecane and Bovine Serum Albumin by Spectroscopy and Computer Simulation Methods. SPECTROSCOPY AND SPECTRAL ANALYSIS, 2021, 41(05): 1487-1492.
