| 光谱学与光谱分析 |
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| Spectroscopic Study on Binding of Folic Acid to Human Serum Albumin |
| LIU Hui-juan, LI Peng, ZHANG Ya-dong, GUO Cao, DENG Jun-yuan, CAI Jian-wei, LIU Bo-li* |
| Key Laboratory of Radiopharmaceuticals (Beijing Normal University), Ministry of Education, School of Chemistry, Beijing Normal University, Beijing 100875, China |
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Abstract The interaction of human serum albumin and folic acid was studied using fluorescence spectroscopy, UV absorption and synchronous fluorescence spectroscopy in the pH 7.4 Tris-HCl buffer system at different temperatures. The research shows that these interactions result in the endogenous fluorescence quenching of HSA, which belongs to a static quenching mechanism. The quenching rate constants, the binding constants and the binding sites of the static quenching were calculated. The distance between the body (HSA) and receptor (folic acid) and the efficiency of energy transfer were obtained to be 1.77 nm and 0.052 65 respectively, based on the theory of Förster nonradiative energy transfer. And according to the thermodynamic parameters calculated the binding of HSA and folic acid is mainly attributed to the hydrophobic interaction, partly static force. Further more the synchronous fluorescence spectrum was utilized to investigate the conformational transformation; The decline result of the hydrophobic nature around Trp demonstrates that the folic acid is in the hydrophobic cavity of HSA.
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Received: 2008-05-12
Accepted: 2008-08-16
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Corresponding Authors:
LIU Bo-li
E-mail: liuboli@bnu.edu.cn
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