葛根素及其衍生物与牛血清白蛋白相互作用研究

采用改造后的Atherton-Todd反应合成了葛根素的两种磷酰化异黄酮, 并应用荧光光谱法研究了葛根素及其磷酰化产物与牛血清白蛋白(BSA)的相互作用. 结果显示葛根素及其磷酰化产物均能与BSA发生相互作用, 但磷酰化产物与蛋白的结合作用相对较弱; 三个小分子对BSA荧光的猝灭是静态猝灭过程, 结合力以疏水作用力为主; 依据能量转移原理求得小分子与BSA间结合距离均小于7 nm. 通过比较葛根素及其磷酰化产物与BSA的相互作用, 初步探讨了三个小分子分子结构与其结合能力之间的联系, 并进一步考察了金属离子对结合反应的影响.

Study on the Interaction of Bovine Serum Albumin with Puerarin and Its Derivatives

In the paper, two new phosphorylated isoflavones of puerarin were successfully obtained by a modified Atheron-Todd reaction. Further, the interactions of bovine serum albumin (BSA) and puerarin or its phosphorylated products were studied under physiological pH by fluorescence spectroscopy. The results showed that puerarin and its phosphorylated products all could form a non-covalent complex with BSA, while the interactions of the phosphorylated isoflavones with BSA were weaker than puerarin. The quench-ing mechanisms of them with BSA were suggested as a static quenching process, and the binding force was mainly a hydrophobic force. The distances between BSA and puerarin and its phosphorylated isoflavones were less than 7 nm according to the theory of the Förster energy transference. The relationship between the molecule structures of these compounds and the binding ability of them with BSA was preliminarily dis-cussed, and the quenching constants in the presence of various metal ions were also explored.