摘要
采用荧光光谱法研究温度对甲砜霉素(Tap)与牛血清白蛋白(BSA)相互作用的机制的影响,结果表明Tap与BSA相互作用的猝灭机制均为静态猝灭;分别计算得出对应温度下Tap与BSA的结合位点和结合常数,通过对热力学参数求解,得出Tap与BSA之间的作用力为氢键与范德华力;利用同步荧光光谱法证明了Tap对BSA的构像有影响.
The effect of temperature on the interaction mechanism of Thiamphenicol(Tap)and Bovine serum albumin(BSA)was studied by fluorescence spectroscopy.The results showed that the quenching mechanism of Tap and BSA was static.The binding sites and binding constants of Tap and BSA at corresponding temperatures were calculated,and the interaction between Tap and BSA was hydrogen bond and Van der Waals force by solving the thermodynamic parameters.The effect of Tap on the structure of BSA was proved by synchronous fluorescence spectrometry.
作者
赵雪卿
王树照
ZHAO Xue-Qing;WANG Shu-Zhao(Department of Chemistry and Chemical Engineering,Lüliang University,Lishi Shanxi 033001,China)
出处
《吕梁学院学报》
2022年第2期12-16,共5页
Journal of Lyuiang University
关键词
甲砜霉素
牛血清白蛋白
荧光光谱
热力学
Thiamphenicol
Bovine serum albumin
fluorescence spectroscopy
thermodynamic
