| 光谱学与光谱分析 |
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| Study on Interaction of Caffeine with Myoglobin by Fluorescence Spectroscopy |
| HUANG He-yong2, 3, GU Xiao-tian1, DING Yan3, ZHOU Jia-hong1, 2, FENG Yu-ying1, 2* |
1. Analysis and Testing Center，Nanjing Normal University, Nanjing 210097, China
2. Key Lab of Biofunctional Materials of Jiangsu Province, Nanjing 210097, China
3. College of Chemistry and Environmental Science, Nanjing Normal University, Nanjing 210097, China |
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Abstract The interaction of caffein and myoglobin was investigated by fluorescence spectroscopy and synchronous fluorescence spectroscopy. The intrinsic fluorescence of myoglobin was significantly quenched by caffein under the physiological condition(pH7.4) .The results indicated that caffeine was capable of binding with myoglobin to form a 1:1 complex and the quenching mechanism of myoglobin affected by caffeine was shown to be a static quenching procedure by calculating quenching constant, binding sites and binding constant. According to the thermodynamic parameters, the main binding force of the interaction is electrostatic force and hydrophobic force. The change in the micro-circumstance of aminos of myoglobin was analyzed by synchronous fluorescence spectrometry. The result indicated that caffeine can change the conformation of the protein, leading to the change in the micro-environment of tryptophane and tyrosine residues from hydrophobic environment to hydrophilic environment to different extent.
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Received: 2008-09-18
Accepted: 2008-12-22
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Corresponding Authors:
FENG Yu-ying
E-mail: yyfeng3@163.com
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