摘要
应用荧光光谱和紫外可见吸收光谱研究了Fe3+介导下的香豆素-3-羧酸(CCA)与牛血清白蛋白(BSA)间的相互作用,确定了Fe3+介导下的CCA对BSA的荧光猝灭过程.在此基础上测定了不同温度下该结合反应的结合常数,结合位点数,热力学参数等,依据能量转移理论确定了CCA和BSA间的结合距离,采用同步荧光技术考察了CCA对BSA构象的影响,并讨论了CCA与BSA的结合模式.结果表明CCA对BSA是动态猝灭过程,结合反应主要是熵驱动,主要作用力是疏水力,香豆素-3-羧酸-Fe3+的加入并未使BSA的构象发生变化.
In view of the influence by iron（Ⅲ ）, the binding between coumarin 3 carbox- ylic acid and Bovine Serum Albumin（BSA） was investigated by fluorescence spectrum and UV spectrum,CCA to BSA fluorescence quenching process in view of the influence by iron（Ⅱ）is proved. The binding constant, the number of binding sites n and thermo- dynamic parameters were measured at different temperatures by fluorescence quenching method. The binding distance between coumarin-3-carboxylic acid and BSA was also ob- tained according to Forster theory of non-radiation energy transfer. The effect of couma- rin 3 carboxylic acid on the conformation of BSA has also been analyzed using synchro- nous fluorescence spectroscopy and the binding mode between coumarin-3-carboxylic acid and BSA was discussed. Experimental results showed that the quenching mecha- nism is dynamic quenching procedure. The binding reaction is mainly entropy drive, the main force is hydrophobic hydraulic, coumarin-3 carboxylic acid-Fe3＋ to join BSA did not make the conformational change.
出处
《华中师范大学学报（自然科学版）》
CAS
北大核心
2013年第4期509-513,518,共6页
Journal of Central China Normal University：Natural Sciences
基金
湖北省自然科学基金项目(2009CDB317)
咸宁学院青年项目(KY11068)
