美他环素与牛血清白蛋白相互作用的光谱研究

利用紫外光谱法、 荧光光谱法研究了美他环素（METC）与牛血清白蛋白（BSA）相互作用的机理； 考察了温度、 溶液酸碱度、 金属离子对METC与BSA相互作用的影响. 实验结果表明， METC对BSA的猝灭属于静态猝灭过程； 它们的结合主要以静电引力为主， 根据Frster非辐射能量转移原理计算了METC与BSA的结合距离; 金属配合物对BSA的猝灭属于静态猝灭过程， 但结合常数相对于在常温时METC直接猝灭BSA的结合常数有很大差异， 而且结合位点数也有相应的改变， 表明金属离子的介入对METC的结构及疏水性能都有不同程度的影响.

Interaction of Metacycline and Bovine Serum Albumin Studied by Spectral Methods

The interaction mechanism of metacycline (METC) and bovine serum albumin (BSA) was studied via fluorescence spectrometry and UV visible absorption spectrometry. The effects of temperature, pH, metal ions on the interaction of METC and BSA were studied. The results indicate that the mechanism of the i nteraction of METC with BSA belongs to static quenching. The major force of binding is static gravitation. Also, the distance of METC BSA was calculated via the Frster theory of non radiation energy transfer. The mechanisms of interactions of metal complexes with BSA also belong to static quenching. The binding constants are different from the constant of the interaction between METC and BSA at room temperature, and the relevant binding sites are changed. It shows that the metal ions affect the structure and hydrophobicity of METC.