Binding Interactions of Hematoporphyrin Monomethyl Ether with Human Serum Albumin
The binding of HMME derivative to human serum albumin(HSA) in aqueous solution was studied using fluorescence spectra and absorption spectra. It was shown that HMME has a powerful ability to quench the HSA fluorescence by a nonradiative energy transfer mechanism.The binding constant K were obtained by fluorescence quenching method. The quenching mechanism of fluorescence of HSA by HMME is a static quenching procedure .The critical binding distance R0 and the energy transfer efficiency E were calculated based on the theory of F(o)ster spectroscopy energy transfer. The binding power is mainly the hydrophobic forces according to the thermodynamic parameters.
Shangyuan Feng Rong Chen Zufang Huang Yongzeng Li Weiwei Chen
Key Laboratory of OptoElectronic Science and Technology for Medicine, Ministry of Education, Fujian Key Laboratory of OptoElectronic Science and Technology for Medicine, Ministry of Education, Fujian
国际会议
北京
英文
980-984
2007-05-23(万方平台首次上网日期,不代表论文的发表时间)