Title :
Binding Interactions of Hematoporphyrin Monomethyl Ether with Human Serum Albumin
Author :
Feng, Shangyuan ; Chen, Rong ; Huang, Zufang ; Li, Yongzeng ; Chen, Weiwei
Abstract :
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 non-radiative 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 Foster spectroscopy energy transfer. The binding power is mainly the hydrophobic forces according to the thermodynamic parameters.
Keywords :
fluorescence; proteins; radiation quenching; ultraviolet spectra; visible spectra; Foster spectroscopy energy transfer; binding constant; critical binding distance; fluorescence quenching method; fluorescence spectra; hematoporphyrin monomethyl ether; human serum albumin; nonradiative energy transfer mechanism; Energy exchange; Fluorescence; Hidden Markov models; Humans; Materials science and technology; Medical diagnostic imaging; Medical treatment; Proteins; Spectroscopy; Thermodynamics;
Conference_Titel :
Complex Medical Engineering, 2007. CME 2007. IEEE/ICME International Conference on
Conference_Location :
Beijing
Print_ISBN :
978-1-4244-1077-4
Electronic_ISBN :
978-1-4244-1078-1
DOI :
10.1109/ICCME.2007.4381885