荧光法对姜黄素与牛血清白蛋白相互作用的研究

Study on the Interaction Between Curcumin and Bovine Serum Albumin by Fluorescence Spectrometry

应用荧光光谱法研究了生理条件下(pH7.4)姜黄素(Curcumin)与牛血清白蛋白(BSA)的相互作用。实验结果表明,姜黄素对BSA产生荧光猝灭作用,其机理属于静态猝灭过程。T=310K时,其猝灭常数为1.388×1012L.mol-1.s-1,表观结合常数为2.387×104L.mol-1。根据Foerster非辐射能量转移理论,测得姜黄素在BSA中的结合位置与色氨酸残基间的距离为4.43nm。探讨了姜黄素对BSA构象的影响及结合机理,考察了体内某些共存金属离子对姜黄素与BSA结合作用的影响。

The interaction between curcumin and bovine serum albumin was studied under the physiological conditions （pH 7. 4 ） by fluorescence spectrometry. The curcumin can quench the fluorescence of bovine serum albumin and the quenching mechanism is static quenching process. At 310K,the quenching constant is 1. 388 × 10^12 L . mol^-1. s^-1 and the apparent binding constant is 2. 387 × 10^4 L. mol^-1. According to the Foerster theory of non-radiation energy transferring, the binding locality of curcumin is measured to be 4. 43nm away from tryptophan residues in BSA. The binding mechanism and the influence of curcumin on BSA confirmation were studied. Furthermore, the effect of some metal ions on the interaction between curcumin and BSA was also investigated.