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| We studied on the Intermolecular Interaction between Perfluorooctanoic Acid and Serum Protein by UV-Fluorescence Spectrometry and the Establishment of the Theoretical Models |
| WANG Yan1, Lü Da2, GUO Ming1, 3*, ZHAO Xiao-xue1 |
1. School of Engineering, Zhejiang A & F University, Lin’an 311300, China
2. School of Forestry and Bio-technology, Zhejiang A & F University, Lin’an 311300, China
3. School of Science, Zhejiang A & F University, Lin’an 311300, China |
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Abstract Study on the establishment of intermolecular interaction between perfluorooctanoic acid (PFOA) and human serum protein (HSA) and its theoretical modeling. Fluorescence spectrums combined with ultraviolet spectrum have been studied the intermolecular interaction between PFOA and HSA to obtain PFOA-HSA ultraviolet-fluorescence spectrum features. The UV-fluorescence characteristic spectra showed that PFOA regularly decreased the UV absorption and fluorescence intensity of HSA, and the maximum emission wavelength of HSA caused obvious blue shift, which indicated that there was intermolecular interaction between PFOA and HSA. The binding constants between PFOA and HSA were obtained by analyzing spectrum experiments data, which indicated the medium intermolecular interaction between PFOA and HSA. On the basis of Van’t Hoff equation to analyze spectrum experiments datas to attain the thermodynamic parameters of the intermolecular interaction between PFOA and HSA. The obtained thermodynamic parameters were ΔH>0, ΔS>0, ΔG<0, which indicated that the main forces between HSA and PFOA were hydrophobic force and hydrogen bond by Ross theories, and the intermolecular interaction between HSA and PFOA was spontaneous process. Synchronous fluorescence spectrum revealed that the intermolecular interaction of PFOA and HSA resulted in a change in the microdomain conformation of the serum protein molecule, which changed the conformational domain of the tryptophan residue. In this paper, the polarizing factor M was proposed to quantitatively characterize the interaction between PFOA and HSA by fluorescence polarization spectroscopy. Based on spectral data analysis, the theoretical model of the interaction between PFOA and HSA was established, The theoretical model results showed that the intermolecular interaction of PFOA and HSA occured mainly in the HSA active site Ⅰ region and the intermolecular interaction between HSA and PFOA was a spontaneous process. The results of spectral experiments were basically consistent with the theoretical modeling results. These data can provide a useful reference for a comprehensive understanding of the intermolecular interactions between biological macromolecules and perfluorinated compounds and the study of microscopic toxicological mechanisms.
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Received: 2017-05-09
Accepted: 2017-10-12
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Corresponding Authors:
GUO Ming
E-mail: guoming@zafu.edu.cn
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