| 光谱学与光谱分析 |
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| Study on Interaction of L-Homocysteine Modified Gold Nanoparticles with Bovine Serum Albumin by Fluorescence Spectroscopy |
| CHEN Hui-hui, ZHU Duan-xu, GUO Yan-li*, WANG Ying, YAN Hong-tao |
| Key Laboratory of Synthetic and Natural Functional Molecule Chemistry of Ministry of Education, College of Chemistry and Materials Science, Northwest University, Xi’an 710069, China |
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Abstract The interaction of L-homocysteine (Cys) modified gold nanoparticles with bovine serum albumin (BSA) was studied by fluorescence quenching spectroscopy and synchronous fluorescence spectra. The binding constant and binding sites of L-homocysteine modified gold nanoparticles to BSA were calculated, respectively, according to the double logarithm regression curve. Fluorescence quenching of BSA by L-homocysteine modified gold nanoparticles was observed, indicating that the quenching mechanism is static quenching. In addition, the thermodynamic data show that the key interaction force is hydrophobic interaction. Finally, the synchronous fluorescence spectra show that the conformation of BSA and the microenvironment of the tryptophan have not obviously changed.
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Received: 2012-05-24
Accepted: 2012-09-08
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Corresponding Authors:
GUO Yan-li
E-mail: guoyl@nwu.edu.cn
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