番泻苷A与牛血清白蛋白相互作用的研究

Study on the Interaction between Sensenoside A and Bovine Serum Albumin

目的研究番泻苷A与牛血清白蛋白之间的相互作用,进一步了解该成分在体内的吸收、转运和分布等过程。方法采用荧光光谱法及紫外光谱法,基于荧光淬灭及非辐射能量转移原理研究番泻苷A和牛血清白蛋白的相互作用机制。结果加入番泻苷A后,BSA的荧光淬灭曲线呈良好的线性关系,且随着温度的升高该淬灭曲线的斜率降低;依据能量转移原理求得其结合距离,由计算结果可知番泻苷A在蛋白上的结合位置距离色氨酸残基均小于7 nm。结论初步判断番泻苷A与蛋白形成了复合物,且此淬灭过程为静态淬灭过程;BSA与淬灭体间均可以发生能量转移,说明牛血清白蛋白与番泻苷A可发生能量转移。

OBJECTIVE To further understand the absorption,transport and distribution of sennaglycosides A in vivo,we researched the interaction of it and bovine serum albumin.METHODS Fluorescence spectrometry and ultraviolet spectroscopy were used to study the mechanism of interaction between sennaglycosides A and bovine serum albumin based on fluorescence quenching and non-radiation energy transfer principles.RESULTS The fluorescence quenching curve of BSA showed a good linear relationship with the addition of valproxine A,and the slope of the quenching curve decreased with the increase of temperature.According to the principle of energy transfer,its binding distance was obtained.From the calculation results,it was known that the binding position of aminoside A on the protein was less than 7 nm from the tryptophan residue.CONCLUSION It is preliminarily determined that sensenoside A formed a complex with the protein,and the quenching process is static quenching process.Energy transfer can occur between BSA and quenched body,indicating that bovine serum albumin and paeonin A can undergo energy transfer.