荧光光谱法研究卡洛磺钠与牛血清白蛋白相互作用特征  

Studies on the Interaction of Carbazochrome Sodium Sulfonate and Bovine Serum Albumin by Spectroscopic Method

作　　者：杨轲[1] 胡志军[2] 于涛[3] 陈建秋[3] 

机构地区：[1]中国药科大学基础化学实验中心,南京21009 [2]江苏省环境科学研究院,南京210036 [3]中国药科大学分析化学教研室,南京210009

出　　处：《海峡药学》2015年第4期230-234,共5页Strait Pharmaceutical Journal

基　　金：国家环保公益性行业科研专项(200809016);江苏省环境工程重点实验室开放基金(KF2009008)

摘　　要：应用荧光光谱和紫外-可见吸收光谱研究了卡洛磺钠(CSS)与牛血清白蛋白(BSA)结合反应的光谱学特征。实验结果表明,在弱酸性条件下CSS对BSA的猝灭机理为动态猝灭,而在中性和弱碱性时则为静态猝灭;根据Frster非辐射能量转移理论计算出310K和p H=7.40时CSS与BSA作用的结合距离为5.18nm;通过计算热力学参数可知,药物与BSA的相互作用是自发过程,且二者之间的主要作用力类型为疏水作用力;此外用同步荧光光谱探讨了CSS对BSA构象的影响。研究还表明常见共存离子对结合反应有较显著的影响。The interaction character of Carbazochrome Sodium Sulfonate （ CSS ） and Bovine serum albumin （ BSA） was investigated by fluorescence spectra and ultra-violet absorption spectra.The results showed that the quenching mechanism of the intrinsic fluorescence of BSA by CSS was a kinetic quenching procedure in the weak acid medium,while the quenching mechanism of that was static quenching procedure in the weak basic or neutral me-dium.The binding site was a distance 5.18 nm away from BSA based on Fφrster snonradiation energy transfer mecha-nism.The thermodynamic parameters showed that the binding power between CSS and BSA was mainly the hydropho-bic interaction.Synchronous spectrum was used to investigate the conformational change of BSA.In addition,the com-mon ions also influence the binding of CSS to BSA.

关 键 词：卡洛磺钠 牛血清白蛋白 相互作用 荧光光谱 紫外-可见光谱 

分 类 号：O657.3[理学—分析化学]