金属离子对花椒毒酚结合牛血清白蛋白体系的影响

doi:10.3969/j.issn.0253-2417.2017.05.010

林产化学与工业 ›› 2017, Vol. 37 ›› Issue (5): 79-87.doi: 10.3969/j.issn.0253-2417.2017.05.010

金属离子对花椒毒酚结合牛血清白蛋白体系的影响

曹洪坤¹, 金晓伟², 张恩风¹, 于慧¹, 石婧楠¹, 边贺东^1,2

1. 广西民族大学化学化工学院;广西林产化学与工程重点实验室, 广西南宁 530006;
2. 广西师范大学化学与药学学院;药用资源化学与药物分子工程教育部重点实验室, 广西桂林 541004

收稿日期:2017-02-22 出版日期:2017-10-25 发布日期:2017-10-30
通讯作者: 边贺东,教授,博士生导师,主要从事配位化学、生物无机研究;E-mail:gxunchem@163.com。 E-mail:gxunchem@163.com
作者简介:曹洪坤(1989-),男,山东淄博人,硕士生,主要从事生物无机研究工作
基金资助:
国家自然科学基金资助项目（21061002，21361003，21101035）

Interactions Between Drugs and Bovine Serum Albumin in the Presence of Metal Ions by Spectral Methods

CAO Hongkun¹, JIN Xiaowei², ZHANG Enfeng¹, YU Hui¹, SHI Jingnan¹, BIAN Hedong^1,2

1. School of Chemistry and Chemical Engineering, Guangxi University for Nationalities;Guangxi Key Laboratory of Chemistry and Engineering of Forest Products, Nan ning 530006, China;
2. School of Chemistry and Phamaceutical Sciences, Guangxi Normal University;Key Laboratory for the Chemistry and Molecular Engineering of Medicinal Resources, Guilin 541004, China

Received:2017-02-22 Online:2017-10-25 Published:2017-10-30

摘要/Abstract

摘要： 运用荧光猝灭光谱（FS）、圆二色光谱（CD）研究了花椒毒酚（XAL）对牛血清白蛋白（BSA）的相互作用以及不同金属离子对XAL-BSA体系的影响。在290、297和304 K的温度下扫描XAL-BSA体系荧光光谱，采用Stern-Volmer方程计算得到各相应温度下XAL对BSA的猝灭速率常数（k_q）分别为6.316×10¹³、4.402×10¹³和3.554×10¹³ L/（mol·s）。研究结果表明：XAL能够猝灭BSA的荧光强度，且猝灭机理为XAL与BSA形成复合物的静态猝灭。在297 K温度下，XAL与BSA的结合常数为3.47×10⁵ L/mol，加入金属离子后对XAL与BSA的结合常数均有不同程度的影响。Föster偶极-偶极非辐射能量转移理论得出：BSA中色氨酸残基与XAL的作用距离（r）为5.29 nm，当加入金属离子后，BSA中色氨酸残基分别与XAL的r均不同程度的降低。圆二色光谱（CD）表明XAL与BSA相互作用后改变了BSA的二级结构，α-螺旋结构的百分比减少，当加入金属离子后，进一步诱导BSA的二级结构变化，α-螺旋结构的百分比进一步减少。

关键词: 花椒毒酚, 牛血清白蛋白, 相互作用

Abstract: The mechanisms of the interaction between xanthotoxol(XAL) and bovine serum albumin(BSA) were investigated by fluorescence and circular dichroism(CD) spectrometry, as well as the effects of common metal ions(Fe³⁺, Cu²⁺, Zn²⁺, Cr³⁺) on the XAL-BSA binding. The quenching constants (k_q) calculated by Stern-Volmer equation under 290,297 and 304 K were 6.316×10¹³,4.402×10¹³ and 3.554×10¹³ L/(mol·s), respectively. The result indicated that XAL could quench the intrinsic fluorescence of BSA strongly, and the quenching mechanism was static quenching process. The binding constant (K) of XAL to BSA at 297 K was 3.47×10⁵ L/mol. The addition of metal ions changed the binding constant. The distance between the tryptophan residues in BSA and XAL was 5.29 nm by using Föster's equation, and it decreased after interaction with metal ions. The CD spectrometry demonstrated that the secondary structure of BSA changed after its interaction with XAL, and α-helix content decreased; the secondary structure of BSA was also changed by addition of metal ions and α-helix content further reduced.

Key words: xanthotoxol, bovine serum albumin, interaction

中图分类号:

TQ35
O657.3

曹洪坤, 金晓伟, 张恩风, 于慧, 石婧楠, 边贺东. 金属离子对花椒毒酚结合牛血清白蛋白体系的影响[J]. 林产化学与工业, 2017, 37(5): 79-87.

CAO Hongkun, JIN Xiaowei, ZHANG Enfeng, YU Hui, SHI Jingnan, BIAN Hedong. Interactions Between Drugs and Bovine Serum Albumin in the Presence of Metal Ions by Spectral Methods[J]. Chemistry and Industry of Forest Products, 2017, 37(5): 79-87.

参考文献

[1] 张新勇,向仁德. 蛇床子化学成分的研究[J]. 中草药,1997(10):588-590. ZHANG X Y,XIANG R D. Study on the chemical constituents of osthol[J].Chinese Traditional and Herbal Drugs,1997(10):588-590.
[2] 张海蓉,边贺东,潘英明,等. 光谱法研究儿茶素与牛血清白蛋白的相互作用[J]. 光谱学与光谱分析,2009,29(11):3052-3056. ZHANG H R,BIAN H D,PAN Y M,et al.Investigation of interaction between catechin and bovine serum albumin by spectroscopic methods[J]. Spectroscopy and Spectral Analysis,2009,29(11):3052-3056.
[3] ZHANG J,YAN Q,LIU J,et al. Study of the interaction between 5-sulfosalicylic acid and bovine serum albumin by fluorescence spectroscopy[J]. Journal of Luminescence,2013,134:747-753.
[4] 易平贵,商志才,俞庆森,等. 丝裂霉素C与牛血清白蛋白结合作用的研究[J]. 化学学报,2000,58(12):1649-1653. YI P G,SHANG Z C,YU Q S,et al.Studies on the interaction between mytomycin C and bovine serum albumin[J].Acta Chimica Sinica,2000,58(12):1649-1653.
[5] ZHONG W,WANG Y,YU J S,et al. The interaction of human serum albumin with a novel antidiabetic agent-SU-118[J]. Journal of Pharmaceutical Sciences,2004,93:1039-1046.
[6] SHAHABADI N,MOHAMMADPOUR M. Study on the interaction of sodium morin-5-sulfonate with bovine serum albumin by spectroscopic techniques[J]. Spectrochimica Acta Part A Molecular & Biomolecular Spectroscopy,2012,86(3):191-195.
[7] 冷晓莲,杨娟,苏波,等. 芦丁对胃蛋白酶部分性质的影响[J]. 天然产物研究与开发,2007,19(2):270-273. LENG X L,YANG J,SU B,et al. The partial influence of rutin on pepsin[J].Natural Product Research and Development,2007,19(2):270-273.
[8] WARE W R. Oxygen quenching of fluorescence in solution:An experimental study of the diffusion process[J]. Journal of Physical Chemistry,1962,66(3):316-320.
[9] CYRIL L. Biochemists' Handbook[M]. London:E. & F. N. Spon Ltd.,1961.
[10] RAHNAMA E,MAHMOODIAN-MOGHADDAM M,KHORSAND-AHMADI S,et al. Binding site identification of metformin to human serum albumin and glycated human serum albumin by spectroscopic and molecular modeling techniques:A comparison study[J]. Journal of Biomolecular Structure and Dynamics,2015,33(3):513-533.
[11] 邵爽,邱瑾. 金属离子对齐多夫定与牛血清白蛋白结合作用的影响[J]. 物理化学学报,2009,25(7):1342-1346. SHAO S,QIU J,Effecting of Metal ions on the interaction between zidovudine and bovine serum albumin[J].Acta Physico-Chimica Sinica,2009,25(7):1342-1346.
[12] YING L,HE W,LIU J,et al. Binding of the bioactive component Jatrorrhizine to human serum albumin[J]. Biochimica Et Biophysica Acta,2005,1722(1):15-21.
[13] REHMAN M T,SHAMSI H,KHAN A U. Insight into the binding mechanism of imipenem to human serum albumin by spectroscopic and computational approaches[J]. Molecular pharmaceutics,2014,11(6):1785-1797.
[14] YUE Y,ZHANG Y,ZHOU L,et al. In vitro study on the binding of herbicide glyphosate to human serum albumin by optical spectroscopy and molecular modeling[J]. Journal of Photochemistry & Photobiology B Biology,2008,90(1):26-32.
[15] LIU J,TIAN J,HE W,et al. Spectrofluorimetric study of the binding of daphnetin to bovine serum albumin[J]. Journal of Pharmaceutical & Biomedical Analysis,2004,35(3):671-677.
[16] GVLER G,VOROB'EV M M,VOGEL V,et al. Proteolytically-induced changes of secondary structural protein conformation of bovine serum albumin monitored by Fourier transform infrared(FT-IR) and UV-circular dichroism spectroscopy[J]. Spectrochimica Acta Part A:Molecular and Biomolecular Spectroscopy,2016,161:8-18.
[17] HU Y J,LIU Y,ZHANG L X,et al. Studies of interaction between colchicine and bovine serum albumin by fluorescence quenching method[J]. Journal of Molecular Structure,2005,750(1/2/3):174-178.

金属离子对花椒毒酚结合牛血清白蛋白体系的影响

Interactions Between Drugs and Bovine Serum Albumin in the Presence of Metal Ions by Spectral Methods

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