葛根素与牛血清白蛋白相互作用的研究

应用荧光光谱法研究了生理条件下(pH7.4)葛根素(PUE)与牛血清白蛋白(BSA)的相互作用。结果表明，葛根素对BSA荧光的猝灭机制属于形成复合物的静态猝灭过程，求得其猝灭常数为7.29×1012 L·mol-1·s-1，结合常数为5.04×104 L·mol-1；根据Frster非辐射能量转移理论，测得葛根素在BSA中的结合位置与色氨酸残基间的距离为3.35 nm；探讨了葛根素对蛋白质空间结构的影响及其相互作用机理；考察了体内某些共存金属离子对葛根素与BSA结合作用的影响。

Studies on the Interaction between Puerarin and Bovine Serum Albumin

The interaction of puerarin and bovine serum albumin (BSA) under physiological condition was studied by fluorospectrophotometry. The experiment demonstrated that the quenching mechanism of puerarin a BSA was static quenching process. The quenching constant is 7.29 x 10(12) L x mol(-1) x s(-1), and the binding constant is 5.04 x 10(4) L x mol(-1). According to the Forster nonradiative energy transfer theory, the binding distance between donor (BSA) and acceptor (puerarin) was calculated to be 3.35 nm. The influence of the presence of puerarin on structure of BSA was studied by synochronous fluorescence method, the binding distance between BSA and puerarin was also measured, and the binding mechanism was discussed. In addition, the effect of some ions on the binding constant of puerarin with BSA was also studied.