合成并表征了丁二酰化壳寡糖铕配合物, 在模拟人体生理条件下, 运用紫外和荧光光谱研究了配合物与牛血清白蛋白(BSA)的相互作用。结果表明: 随着配合物浓度的增加, BSA的紫外光谱表现出增色效应并伴有蓝移;配合物与BSA形成复合物, 从而猝灭BSA内源荧光, 该猝灭机制为静态猝灭。计算得到室温下配合物与BSA的结合常数和结合位点数分别为2.068 2×104 L·mol-1和1.094 72。

Succinic-oligochitosan-Eu(Ⅲ) complex was synthesized and characterized. Under simulated physiological conditions, the interaction between complex and bovine serum albumins (BSA) was studied by ultraviolet spectrum and fluorescence spectrum. The results showed that the absorption intensity of BSA increased with the concentration of complex. The complex quenched the fluorescence of BSA and it was static quenching, and then the binding constant and binding sites were calculated. They were 2.068 2×104 L·mol-1 and 1.094 72 at room temperature, respectively.