Department of Chemistry and Center of Analysis and Testing, Nanchang University, Nanchang 330031, Jiangxi, PR China.
Spectrochim Acta A Mol Biomol Spectrosc. 2010 Oct 1;77(2):430-6. doi: 10.1016/j.saa.2010.06.010. Epub 2010 Jun 11.
A new Schiff-base compound, N'-(2-hydroxynaphthalenemethylene)-4-(2-hydroxyl naphthalenemethylenamine)benzoylhydrazine (1), was synthesized and the interaction between zinc complex (1-Zn) and bovine serum albumin (BSA) was investigated by fluorescence and absorption spectroscopies. A marked increase in the fluorescence intensity of 1-Zn was observed at 475 nm upon addition of BSA when excitation wavelength was set at 370 nm in pH 7.4 Tris-HCl buffer solution. Reversely, the intrinsic fluorescence of BSA could be quenched by 1-Zn complex. The quenching mechanism was suggested as static quenching according to the Stern-Volmer equation and the UV-vis absorption spectral change of 1-Zn upon addition of BSA. The binding constants K(b) and the number of binding sites n were calculated. The effect of 1-Zn on the conformation of BSA was studied using synchronous fluorescence spectroscopy and three-dimensional fluorescence spectroscopy. In addition, the binding average distance r between the donor (BSA) and acceptor (1-Zn) was estimated based on the Förster's non-radiation energy transfer theory.
合成了一种新的席夫碱化合物 N'-(2-羟基萘亚甲基)-4-(2-羟基萘亚甲基胺)苯甲酰腙（1），并通过荧光和吸收光谱研究了锌配合物（1-Zn）与牛血清白蛋白（BSA）之间的相互作用。在 pH 7.4 的 Tris-HCl 缓冲溶液中，当激发波长设置为 370nm 时，BSA 的加入使 1-Zn 的荧光强度在 475nm 处显著增加。相反，1-Zn 复合物可以猝灭 BSA 的固有荧光。根据 Stern-Volmer 方程和 1-Zn 加入 BSA 时的紫外可见吸收光谱变化，猝灭机制被认为是静态猝灭。计算了结合常数 K(b)和结合位点数 n。使用同步荧光光谱和三维荧光光谱研究了 1-Zn 对 BSA 构象的影响。此外，根据福斯特非辐射能量转移理论，估算了供体（BSA）和受体（1-Zn）之间的结合平均距离 r。
