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采用荧光光谱法和紫外吸收光谱法研究了灯盏花素(BR)与牛血清白蛋白(BSA)的相互作用;利用热力学方程计算了295K和308K下的热力学参数ΔH、ΔG和ΔS,根据Stern-Volmer方程求出了猝灭常数和结合常数.结果表明,BR对BSA的荧光具有猝灭作用,其猝灭机制为动态-静态联合猝灭,BSA发射峰略有蓝移.BR与BSA之间的作用力主要为疏水作用.
The interaction between breviscapine (BR) and bovine serum albumin (BSA) was studied by fluorescence spectroscopy and ultraviolet absorption spectroscopy. The thermodynamic parameters ΔH, ΔG and ΔS at 295K and 308K were calculated by thermodynamic equations. According to Stern- Volmer equation was used to determine the quenching constants and binding constants. The results showed that BR quenched the fluorescence of BSA, the quenching mechanism was dynamic-static quenching, and the BSA emission peak was slightly blue-shifted. Between BR and BSA The main force of the hydrophobic effect.