Binding interactions of hematoporphyrin monomethyl ether with human serum albumin

被引：0

作者：

Feng, Shangyuan ^{[1
]}

Chen, Rong ^{[1
]}

Huang, Zufang ^{[1
]}

Li, Yongzeng ^{[1
]}

Chen, Weiwei ^{[1
]}

机构：

[1] Fujian Normal Univ, Minist Educ, Key Lab Optoelect Sci & Technol Med, Fuzhou 350007, Peoples R China

来源：

2007 IEEE/ICME INTERNATIONAL CONFERENCE ON COMPLEX MEDICAL ENGINEERING, VOLS 1-4 | 2007年

关键词：

D O I：

10.1109/ICCME.2007.4381885

中图分类号：

R318 [生物医学工程];

学科分类号：

0831 ;

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 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 R-0 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.

引用

页码：974 / 978

页数：5

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