摘要
用荧光光谱和质谱研究了对硝基苯胺(PNA)与牛血清白蛋白(BSA)的相互作用。结果表明,对硝基苯胺能与BSA相结合,结合后对硝基苯胺的ESI-MS选择正离子峰明显减弱,并有规律地猝灭BSA的内源荧光,其机理属静态猝灭过程。实验获得了不同温度下,对硝基苯胺与BSA作用的结合常数和热力学参数,根据所得结果可推断对硝基苯胺与BSA的主要作用力为疏水作用力。由F rster非辐射能量转移理论计算得出了对硝基苯胺与BSA结合位置的距离。采用同步荧光研究发现,对硝基苯胺能进入BSA的疏水区,从而对BSA的构象产生一定的影响,这与对硝基苯胺的生物毒性有关。
The interaction of p-nitroaniline （PNA） with bovine serum albumin （BSA） was studied by fluorescence spectrometric and mass spectrometric methods. The positive selective ion peak of PNA in ESI-MS decreased after PNA binding with BSA. And with increasing content of PNA, the quenching spectra of BSA could be observed under different conditions. The results indicated that BSA could combine with p-nitroaniline, and form stable complex of BSA-PNA which resulted in the static quenching mechanism. Some binding constants and thermodynamic parameters of BSA and p-nitroaniline were obtained at different temperatures. The distance of their binding sites were determined according to the theory of Forster＇s non-radiative energy transfer. Based on the above results, it could be concluded that the hydrophobic interaction between BSA and PNA was the main combination forces. Meanwhile, the effect of p-nitroaniline on the conformation of BSA was also studied using synchronous fluorescence spectrometry, and it was found that the PNA could penetrate into the hydrophobic zone of BSA and affect the conformation, which related to the biochemical toxicity of PNA.
出处
《分析科学学报》
CAS
CSCD
北大核心
2009年第1期36-40,共5页
Journal of Analytical Science
基金
江西省教育厅基金(No.JJ2007-18)
关键词
荧光光谱
质谱
对硝基苯胺
牛血清白蛋白
相互作用
Fluorescence spectroscopy
Mass spectrometry
p-nitroaniline
Bovine serum albumin
Interaction
