Abstract：The binding reaction of methyl pheophorbide-a with bovine serum albumins (BSA) in aqueous solution was studied by fluorescence and UV-Vis absorption spectra. The results indicated that the combination reaction of them was a single static quenching process. In aqueous solution, methyl pheophorbide-a strongly bound BSA with the apparent molar ratio of 2∶1 because of methyl pheophorbide-a polymerized by itself. The binding constant KB was 6.7×104 L·mol-1. In mixture solvent of tetrahydrofuran and water, methyl pheophorbide-a existed as single molecule and bound BSA with a molar ratio of 1∶1. There is single position for combining methyl pheophorbide-a with BSA. The shortest binding distance (r=3.50 nm) and energy transfer efficiencies (E=0.39) between donor (BSA) and acceptor (methyl pheophorbide-a) were obtained by Frster′s nonradiative energy transfer mechanism.
刘永明，王进军，邬旭然. 脱镁叶绿酸-a甲酯的合成及对牛血清白蛋白的结合作用[J]. 光谱学与光谱分析, 2005, 25(05): 747-750.
LIU Yong-ming,WANG Jin-jun,WU Xu-ran. Study on the Interaction of Methyl Pheophorbide-a and Bovine Serum Albumins by Fluorescence. SPECTROSCOPY AND SPECTRAL ANALYSIS, 2005, 25(05): 747-750.
