Binding Interactions of Hematoporphyrin Monomethyl Ether with Human Serum Albumin

摘要：

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.

作者: Shangyuan Feng Rong Chen Zufang Huang Yongzeng Li Weiwei Chen

作者单位: 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

会议类型: 国际会议

会议名称: 2007 IEEE/ICME International Conference on Complex Medical Engineering-CME2007(CME2007 第二届国际复合医学工程学术大会)

会议地点: 北京

会议语种:英文

页码: 980-984

在线出版日期: 2007-05-23（万方平台首次上网日期，不代表论文的发表时间）