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荧光光谱法研究四苯基-锌金属卟啉与蛋白质的相互作用机理

Study on Interaction Mechanism between Meso-Tetra-(4-Hydroxyphenyl)-Zn Porphyrin and Bovine Serum Albumin by Fluorescence Method

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摘要

利用荧光光度法研究了meso-四(4-羟基苯基)卟啉-锌金属卟啉(TPP-Zn)与牛血清白蛋白(BSA)之间的结合反应。TPP-Zn对于BSA有荧光猝灭作用,基于TPP-Zn对BSA内源荧光的猝灭机理,测定了两者之间在不同温度下的结合常数,温度在27,35和42℃时,利用荧光猝灭法测得的结合常数K分别为1.521×106 L·mol-1,7.048×105 L·mol-1,1.473×105 L·mol-1,各温度下的最大扩散碰撞猝灭速率常数Kq均大于2.0×1010 L·mol-1·s-1,由此判定猝灭类型为静态猝灭。根据Frster非辐射能量转移理论,确定了TPP-Zn与BSA之间的能量转移效率E,能量给体(BSA)与受体(TPP-Zn)之间的结合距离r=3.72<7 nm,符合非辐射能量转移条件。依据热力学参数ΔG<0,ΔH<0和ΔS>0确定了TPP-Zn与BSA之间的作用力主要是静电引力。

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 Frster 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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中图分类号:O657

DOI:10.3964/j.issn.1000-0593(2009)03-0773-04

基金项目:国家自然科学基金项目(20577016),山东省自然科学基金项目(Y2006B36)和山东省自然科学基金项目(Y2008B44)资助。

收稿日期:2008-05-10

修改稿日期:2008-08-06

网络出版日期:0001-01-01

作者单位    点击查看

张丽娜:济南大学 化学与化工学院,山东 济南 250022
陈欣:济南大学 化学与化工学院,山东 济南 250022
夏阳:济南大学 化学与化工学院,山东 济南 250022
吴丹:济南大学 化学与化工学院,山东 济南 250022
于京华:济南大学 化学与化工学院,山东 济南 250022
杜斌:济南大学 化学与化工学院,山东 济南 250022
魏琴:济南大学 化学与化工学院,山东 济南 250022

联系人作者:魏琴(sdjndxwq@163.com)

备注:魏琴|教授|女,1961年生,济南大学化学与化工学院。

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引用该论文

ZHANG Li-na,CHEN Xin,XIA Yang,WU Dan,YU Jing-hua,DU Bin,WEI Qin. Study on Interaction Mechanism between Meso-Tetra-(4-Hydroxyphenyl)-Zn Porphyrin and Bovine Serum Albumin by Fluorescence Method[J]. Spectroscopy and Spectral Analysis, 2009, 29(3): 773-776

张丽娜,陈欣,夏阳,吴丹,于京华,杜斌,魏琴. 荧光光谱法研究四苯基-锌金属卟啉与蛋白质的相互作用机理[J]. 光谱学与光谱分析, 2009, 29(3): 773-776

被引情况

【1】俞波,兰秀风,张林,邹如萍,陈奇. 法莫替丁与牛血清蛋白相互作用的光谱研究. 激光与光电子学进展, 2018, 55(4): 43003--1

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