Sheng Liang-quan, Yan Xiang-yang, Xu Hua-jie, Tong Hong-wu, Liu Shao-min
Department of Chemistry, Fuyang Teachers College, Fuyang 236041, China.
Guang Pu Xue Yu Guang Pu Fen Xi. 2007 Feb;27(2):306-8.
The interaction of BSA and NIC was investigated by absorption spectra, fluorescence spectroscopy and synchronous fluorescence spectroscopy. In the system of sodium phosphate dibasic-citric acid of 0.1 mol(-1) x L(-1), fluorescence titration showed that the fluorescence intensity of BSA at 342 nm was quenched when NIC was added, NIC was capable of binding with BSA to form a 1:1 complex and the quenching mechanism of BSA affected by NIC was shown to be a static quenching procedure by calculating the binding number n and binding constant K. NIC decreased the intensity of the characteristic absorption peak of BSA, showing that the binding of NIC to BSA had strong impact on protein conformation with the decrease in a-helical content of the protein. Synchronous fluorescence indicated that the binding of NIC to BSA is near tryptophan subunit.
通过吸收光谱、荧光光谱和同步荧光光谱研究了牛血清白蛋白（BSA）与尼古丁（NIC）的相互作用。在0.1 mol(-1) x L(-1)的磷酸氢二钠-柠檬酸体系中，荧光滴定表明，加入NIC后，BSA在342 nm处的荧光强度猝灭，NIC能够与BSA结合形成1:1复合物，通过计算结合数n和结合常数K表明，NIC对BSA的猝灭机制为静态猝灭过程。NIC降低了BSA特征吸收峰的强度，表明NIC与BSA的结合对蛋白质构象有强烈影响，蛋白质的α-螺旋含量降低。同步荧光表明，NIC与BSA的结合靠近色氨酸亚基。
