6-糠氨基嘌呤与牛血清白蛋白相互作用的研究

Study on the Interaction between 6-Furfurylaminopurine and Bovine Serum Albumin by Fluorescence

应用荧光光谱法研究了6-糠氨基嘌呤(KT)与牛血清白蛋白(BSA)相互作用的光谱特性。测定了16℃、28℃和39℃不同温度下的结合常数KA分别为:2.43×104、1.33×104、1.22×104L/mol,结合位点数n分别为:1.08、1.02、1.02。研究结果表明:KT对BSA内源荧光的猝灭机理主要为静态猝灭;探讨了相互作用机理,KT主要以静电作用与BSA相互作用;研究了KT对BSA构象的影响,表明BSA的荧光主要源于色氨酸残基,KT对BSA的构象有影响。

The interaction between 6-furfurylaminopurine and bovine serum albumin （BSA） were studied by fluorescence. The binding constants KA and binding sites n were measured at different temperatures （16℃ ：KA=2. 432 × 10^4 L·mol^-1,n=1. 077; 28℃ ：KA =1. 332 × 10^4 L·mol^-1,n= 1. 024; 39℃：KA= 1. 220× 10^4 L·mol^-1, n=1. 016）. The experimental results revealed that 6-furfurylaminopurine has strong ability to quench the intrinsic fluorescence of BSA and the interactions has been verified as consistent with the static quenching procedure. According thermodynamic parameters, the interaction forces was determined to be electrostatic force.