| 光谱学与光谱分析 |
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| Study on Interaction Mechanism between Meso-Tetra-(4-Hydroxyphenyl)-Zn Porphyrin and Bovine Serum Albumin by Fluorescence Method |
| ZHANG Li-na, CHEN Xin, XIA Yang, WU Dan, YU Jing-hua, DU Bin, WEI Qin |
| School of Chemistry and Chemical Engineering, University of Jinan, Ji’nan 250022, China |
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Abstract In the present paper, the binding reaction between meso-tetra-(4-hydroxyphenyl)-Zn porphyrin (TPP-Zn) and bovine serum albumin (BSA) was studied at different temperatures by fluorescence method. It was shown that meso-tetra-(4-hydroxyphenyl)-Zn porphyrin has a strong ability of quenching the fluorescence of bovine serum albumin. Based on the mechanisms of fluorescence quenching of bovine serum albumin caused by meso-tetra-(4-hydroxyphenyl)-Zn porphyrin, the binding constants between meso-tetra-(4-hydroxyphenyl)-Zn porphyrin and bovine serum albumin were measured under different temperatures. The experiment showed that meso-tetra-(4-hydroxyphenyl)-Zn porphyrin and bovine serum albumin have strong interactions. The binding constants of the reaction at 27 ℃, 35 ℃ and 42 ℃ were 1.521×106 L·mol-1,7.048×105 L·mol-1 and 1.473×105 L·mol-1,respectively, and were decreased with increasing the temperature. The constants of maximum diffusion collision quenching rate-Kq were above 2.0×1010 L·mol-1·s-1. Therefore, the sort of quenching between meso-tetra-(4-hydroxyphenyl)-Zn porphyrin and bovine serum albumin was determined as static quenching. By the theory of Frster of non-radiation energy transfer, the binding distance and the energy transfer efficiency at 27 ℃ between meso-tetra-(4-hydroxyphenyl)-Zn porphyrin (accepter of energy) and bovine serum albumin (donor of energy) were obtained, respectively. The binding distance was 3.72 nm, which is less than 7 nm, therefore, the interaction was similar to the non-radiation energy transfer, and the static quenching was further proved. According to the thermodynamic parameters, the main sorts of binding force between meso-tetra-(4-hydroxyphenyl)-Zn porphyrin and bovine serum albumin could be judged as electrostatic force when ΔG＜0, ΔH＜0 and ΔS＞0.
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Received: 2008-05-10
Accepted: 2008-08-06
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Corresponding Authors:
ZHANG Li-na
E-mail: sdjndxwq@163.com
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