The interaction between lanthanide cationic porphyrin and bovine serum albumin （BSA） was studied by fluorescence and UV-Vis spectrum. The static quenching of BSA was observed in the presence of YbTMPyP. According to...The interaction between lanthanide cationic porphyrin and bovine serum albumin （BSA） was studied by fluorescence and UV-Vis spectrum. The static quenching of BSA was observed in the presence of YbTMPyP. According to the thermodynamic parameters, this binding was regarded as ＂enthalpy-driven＂ reaction. Furthermore, YbTMPyP is so close to the residues of BSA that molecular resonance energy transfer occurs between them. Besides, the red drift and hypochromicity of absorption spectrum of YbTMPyP were accompanied with the binding reaction.展开更多
基金Project supported by the National Natural Science Foundation of China （No. 30570015） and 0pen Fund of State Key Laboratory of Agricultural Microbiology （Huazhong Agricultural University）.
文摘The interaction between lanthanide cationic porphyrin and bovine serum albumin （BSA） was studied by fluorescence and UV-Vis spectrum. The static quenching of BSA was observed in the presence of YbTMPyP. According to the thermodynamic parameters, this binding was regarded as ＂enthalpy-driven＂ reaction. Furthermore, YbTMPyP is so close to the residues of BSA that molecular resonance energy transfer occurs between them. Besides, the red drift and hypochromicity of absorption spectrum of YbTMPyP were accompanied with the binding reaction.
