灿烂绿与牛血清白蛋白相互作用的研究

Study on the Interaction between Brilliant Green and Bovine Serum Albumin

用荧光光谱法、紫外光谱法研究了灿烂绿(BG)与牛血清白蛋白(BSA)相互作用的光谱特性。测定了BG与BSA在16℃、30℃、45℃三个温度下的结合常数KA和结合位点数n。结果表明:BG对BSA内源荧光的猝灭主要为静态猝灭;以范德华力或氢键作用力与牛血清白蛋白相互作用。研究了BG对BSA的构象的影响。

The interactions between brilliant green and bovine serum albumin （BSA） were studied by fluorescence and ultraviolet-visible absorption spectroscopy. The binding constants KA （16℃ ：6. 352× 10^4 L·mol^-1,30℃：2. 162×10^4 L·mol^-1,45℃：1. 150×10^4 L·mol ^-1） and binding sites n（16℃：1.07, 30℃ ：0. 98,45℃：0. 92） were measured at different temperatures. The experimental results indicated that brilliant green had strong ability to quench the intrinsic fluorescence of BSA and the interactions had been verified as consistent with the static quenching procedure. According to the thermodynamic parameters the interaction force was determined to be vander Waals force. Based on the mechanism of the F6rster energy transference, the transfer efficiency of energy E and transfer distance r between acceptor brilliant green and donor BSA were obtained at different temperatures, and they are E = 0. 2153,r=3.17 nm（16℃） ;E=0. 2072, r=3.27 nm（30℃） and E=0. 2350, r=3.04 nm（45℃）.