有机磷钨多金属氧酸盐FSPW与牛血清白蛋白相互作用

王帅帅;刘霞

doi:10.3981/j.issn.1000-7857.2011.04.002

科技导报 >

2011 , Vol. 29 >Issue 11-04: 25 - 29

DOI: https://doi.org/10.3981/j.issn.1000-7857.2011.04.002

研究论文

有机磷钨多金属氧酸盐FSPW与牛血清白蛋白相互作用

王帅帅;刘霞

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1. 北京理工大学机电学院，北京 1000812. 中国农业大学理学院，北京 100193

收稿日期: 2010-08-16

修回日期: 2011-01-12

网络出版日期: 2011-02-08

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Interaction Between K10C4H4FN2O2Sm(PW11O39)2·12.5H2O and Bovine Serum Albumin

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Received date: 2010-08-16

Revised date: 2011-01-12

Online published: 2011-02-08

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摘要

利用紫外-可见吸收光谱和荧光光谱法，考查了有机磷钨多金属氧酸盐K10C4H4FN2O2Sm(PW11O39)2·12.5H2O（FSPW）与牛血清白蛋白（BSA）间的相互作用。实验表明，化合物FSPW引起BSA蛋白质荧光强度发生有规律猝灭。结合紫外-可见吸收光谱的结果可以判断，化合物FSPW对BSA的荧光猝灭是与BSA基态分子间发生作用的结果，与BSA结合反应的猝灭机制为静态猝灭。化合物FSPW与BSA相互作用的?驻G<0，表明它与BSA的结合平衡是一个自发的过程。?驻H<0、?驻S<0说明化合物FSPW与BSA的作用过程是一个放热过程，与BSA的相互作用主要是焓驱动的结果。化合物FSPW主要通过氢键和范德华力与BSA发生相互作用。同步荧光光谱表明，化合物FSPW与BSA发生了强结合并进入蛋白质的疏水腔，导致蛋白质的构象发生变化，结合位点接近于色氨酸残基。

关键词： 多金属氧酸盐; 5-氟尿嘧啶; 稀土; 牛血清白蛋白; 荧光光谱

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王帅帅;刘霞 . 有机磷钨多金属氧酸盐FSPW与牛血清白蛋白相互作用[J]. 科技导报, 2011 , 29(11-04) : 25 -29 . DOI: 10.3981/j.issn.1000-7857.2011.04.002

Abstract

The interaction between the polyoxometalate K10C4H4FN2O2Sm(PW11O39)2·12.5H2O (FSPW) and Bovine Serum Albumin (BSA) was investigated by using fluorescence and UV/vis. The experimental results show that the regular fluorescence quenching of BSA is caused by the compound FSPW. According to the UV-visible absorption spectra, the fluorescence quenching of BSA is caused by the formation of FSPW-BSA complex, and it is a static quenching. The ?驻G of the process of interaction between the compound FSPW and BSA is less than zero, which indicates that this process is a spontaneous process. The ?驻H and ?驻S are both less than zero, which shows that the binding process of FSPW and BSA is an exothermic molecular interaction, in which the hydrogen bond and van der Waals' force play the major role. The results of synchronous fluorescence spectroscopy show that FSPW is strongly bound with BSA by inserting into the hydrophobic cavity of the protein, and the binding process causes the change of protein conformation. The binding site is close to the tryptophan residue.

Key words： polyoxometalate; 5-fluorouracil; rare earth; bovine serum albumin; fluorescence quenching

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