荧光光谱法研究山姜素与牛血清白蛋白的相互作用机理
Study on the Interaction Mechanism of Alpinetin with Bovine Serum Albumin by Fluorescence Spectroscopy
摘 要
研究了模拟生理条件下,山姜素与牛血清白蛋白(BSA)的相互作用。山姜素猝灭BSA为静态猝灭过程,获得了不同温度下山姜素与BSA的结合常数和结合位点数。考察了Mg2+、Ca2+、Zn2+、Cu2+等金属离子对结合作用的影响。热力学参数研究发现静电作用力为山姜素与BSA的主要结合力。根据Frster非辐射能量转移理论,计算了山姜素与BSA之间的结合距离r0为4.07 nm。同步荧光光谱法研究结果表明山姜素对酪氨酸残基的微环境产生了影响,使其疏水性增强,而对色氨酸残基的微环境没有产生影响。
山姜素
牛血清白蛋白
荧光猝灭
Synchronous fluorescence spectroscopy
Alpinetin
Bovine serum albumin
Fluorescence quenching
Abstract
The interaction between alpinetin and bovine serum albumin (BSA) was studied under simulated physiological conditions. Alpinetin quenches the fluorescence of BSA via a static quenching process. The binding affinity and number of binding sites were measured at different temperatures. Effects of Mg2+, Ca2+, Zn2+ and Cu2+ on the binding were also studied. Thermodynamic parameters obtained revealed that electrostatic interaction is the primary force between alpinetin and BSA. According to Frster′s non-radiative energy transfer theory, the distance r0 between alpinetin and BSA found was calculated to be 4.07 nm. The synchronous fluorescence spectra showed the vicinity of tyrosine residue become more hydrophobicity, which no effect was found surrounding the tryptophan residue.
中图分类号 O657.31
所属栏目 试验与研究
基金项目 吉林省科技厅项目(20140101023JC);吉林省教育厅“十二五”科技项目(20140257);长春师范大学研究生创新基金(cscxy2013008)
收稿日期 2013/11/28
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联系人作者赵婷婷(sybi@sina.com)
备注赵婷婷(1990-),女,吉林松原人,硕士研究生,从事光谱分析化学研究。
引用该论文: ZHAO Ting-ting,BI Shu-yun,WANG Yu,WANG Tian-jiao. Study on the Interaction Mechanism of Alpinetin with Bovine Serum Albumin by Fluorescence Spectroscopy[J]. Physical Testing and Chemical Analysis part B:Chemical Analysis, 2014, 50(8): 944～948
赵婷婷,毕淑云,王瑜,王天娇. 荧光光谱法研究山姜素与牛血清白蛋白的相互作用机理[J]. 理化检验－化学分册, 2014, 50(8): 944～948
被引情况:
【1】陈毅挺,李艳霞,黄露,庄婷娟,林棋, "维生素K3的解离常数测定及其与牛血清白蛋白的相互作用",理化检验－化学分册 52, 61-65(2016)
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参考文献
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【2】韩二伟,王瑞玲,徐丽繁,等.2-(4-甲基苯基-3-(N-乙酰基)-5-(2-羟基苯基)-1,3,4-噁唑啉的合成及与人血清白蛋白的相互作用［J］.理化检验-化学分册, 2013,49(6):633-638.
【3】毕淑云,边江鱼.分子光谱法研究美他环素与人血清白蛋白的相互作用［J］.分子科学学报, 2010,26(2):99-102.
【4】廉淑芹,杨冬芝,郑笑笑,等.应用荧光光度法研究加替沙星与胃蛋白酶的相互作用［J］.理化检验-化学分册, 2013,49(3):253-255.
【5】欧阳运富,王永生,李贵英.1-羟基芘与牛血清白蛋白的相互作用［J］.理化检验-化学分册, 2011,47(3):253-256.
【6】WANG Zhen, CHEN Jun-hui, WANG Shao-bin, et al. Characterizing the interaction between oridonin and bovine serum albumin by a hybrid spectroscopic approach［J］. Journal of Luminescence, 2013,134:863-869.
【7】ZHANG Guo-wen, ZHAO Nan, HU Xing, et al. Interaction of alpinetin with bovine serum albumin: probing of the mechanism and binding site by spectroscopic methods［J］. Spectrochimica Acta Part A, 2010,76:410-417.
【8】STERINER R F, WEINRYB I. Excited states of protein and nucleic acid［M］. New York: Plenum Press, 1971:40.
【9】LAKOWICZ J R. Principles of fluorescence spectroscopy［M］. New York: Plenum Press, 1999:237.
【10】WARE W R. Oxygen quenching of fluorescence in solution: an experimental study of the diffusion process［J］. Journal of Physical Chemistry, 1962,66:455-458.
【11】BI Shu-yun, SONG Da-qian, KAN Yu-he. Spectroscopic characterization of effective components anthraquinones in chinese medicinal herbs binding with serum albumins［J］. Spectrochimica Acta Part A, 2005,62(1):203-212.
【12】ROSS P D, SABRAMAMIAN S. Thermodynamics of protein association reactions forces contributing to stabiliby［J］. Biochemistry, 1981,20:3096-3102.
【13】FORSTER T. Intermolecular energy migration and fluorescence［J］. Annals of Physics, 1948,2:55-57.
【14】SUZUKIDA M, LE H P, SHAHID F. Resonance energy transfer between cysteine-34 and tryptophan-214 in human serum albumin. distance measurements as a function of pH［J］. Biochemistry, 1983,22(10):2415-2420.
【15】陈国珍,黄贤智,许金钩,等.荧光分析法［M］.2版.北京:科学出版社, 1990:123.
【16】VALEUR B, BROCHON J C. New trends in fluorescence spectroscopy［M］. Berlin: Springer Press, 1999:25.
【17】YUAN Tao, WELJIE A M, VLIGEL H J. Typtophan fluorescence quenching by methionine and selenomethionine residues of calmodulin: orientation of peptide and protein binding［J］. Biochemistry, 1998,37:3187-3195.
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