在模拟生理条件下,利用分子荧光光谱、紫外-可见吸收光谱以及瑞利散射光谱研究了Tl(Ⅲ)离子与人血清白蛋白(HSA)的相互作用。实验结果指出,Tl(Ⅲ)离子对蛋白质的猝灭是由于生成了新的基态复合物,属于静态猝灭过程。此外,还计算了二者结合反应的结合常数、结合位点数和热力学参数。最后,利用同步荧光光谱探究了Tl(Ⅲ)离子对蛋白质构象的影响。 Under simulated physiological conditions, the interaction between Tl (Ⅲ) ion and human serum albumin (HSA) was studied by molecular fluorescence spectroscopy, UV-Vis absorption spectroscopy and Rayleigh scattering spectroscopy. The experimental results indicate that the quenching of protein by Tl (Ⅲ) ions is due to the formation of a new ground state complex, which belongs to the static quenching process. In addition, the binding constants, binding sites and thermodynamic parameters were also calculated. Finally, the effect of Tl (III) ions on the conformation of the protein was explored using synchronous fluorescence spectroscopy.