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化学学报 >

2012 , Vol. 70 >Issue 15: 1617 - 1624

DOI: https://doi.org/10.6023/A12040114

研究论文

氧钒配合物[VO(o-Van-Asn)(Phen)]·1.5CH3OH的合成、晶体结构及与DNA和BSA的相互作用

  • 郭琼 ,
  • 李连之 ,
  • 董建方 ,
  • 刘鸿雁 ,
  • 薛泽春 ,
  • 许涛
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  • a 聊城大学化学化工学院 聊城 252059;
    b 山东工程技师学院材料科学系 聊城 252027

收稿日期: 2012-04-13

  网络出版日期: 2012-05-23

基金资助

项目受山东省自然科学基金(No. Y2004B02)资助.

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Synthesis, Crystal Structure and Interactions with DNA and BSA of a Oxovanadium(IV) Complex [VO(o-Van-Asn)(Phen)]?1.5CH3OH

  • Guo Qiong ,
  • Li Lianzhi ,
  • Dong Jianfang ,
  • Liu Hongyan ,
  • Xue Zechun ,
  • Xu Tao
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  • a School of Chemistry and Chemical Engineering, Liaocheng University, Liaocheng 252059;
    b Department of Material Science, Shandong Polytechnic Technician College, Liaocheng 252027

Received date: 2012-04-13

  Online published: 2012-05-23

Supported by

Project supported by the Natural Science Foundation of Shandong Province (No. Y2004B02).

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摘要

合成了一种新的L-天冬酰胺邻香草醛席夫碱和1,10-邻菲咯啉的氧钒配合物[VO(o-Van-L-Asn)(Phen)]· 1.5CH3OH (o-Van-L-Asn＝邻香草醛与L-天冬酰胺形成的席夫碱, Phen＝1,10-邻菲咯啉). 利用红外光谱对其进行了表征, 并通过X射线单晶衍射测定了其晶体结构. 该晶体属于三斜晶系, P-1空间群, 晶胞参数为: a＝0.98990(10) nm, b＝1.21591(11) nm, c＝1.28349(12) nm, α＝66.8180(10)°, β＝83.816(2)o, γ＝66.4150(10)o, V＝1.2992(2) nm3, Dc＝1.430 g· cm-3, Z＝1, F(000)＝580, R1＝0.0626, wR2＝0.1631. 通过紫外吸收光谱、荧光光谱、圆二色光谱(CD)和粘度测定等方法研究了该配合物与小牛胸腺DNA (CT-DNA)的相互作用. 结果表明, 配合物以插入方式与CT-DNA结合. 光谱法研究该配合物与牛血清白蛋白(BSA)的相互作用表明, 它主要以静态猝灭方式使BSA的内源性荧光发生猝灭, 可引起蛋白构象的变化. 计算得到了其结合常数Kb和结合位点数n.

关键词： 氧钒配合物; L-天冬酰胺席夫碱; 晶体结构; DNA; BSA

本文引用格式

郭琼 , 李连之 , 董建方 , 刘鸿雁 , 薛泽春 , 许涛 . 氧钒配合物[VO(o-Van-Asn)(Phen)]·1.5CH3OH的合成、晶体结构及与DNA和BSA的相互作用[J]. 化学学报, 2012 , 70(15) : 1617 -1624 . DOI: 10.6023/A12040114

Abstract

A new oxovanadium(IV) complex, [VO(o-Van-Asn)(Phen)]·1.5CH3OH (o-Van-Asn is the Schiff base derived from o-vanillin and L-asparagine, Phen＝1,10-phenanthroline) has been synthesized. In the synthetic procedure of title complex, a methanol solution of o-vanillin (0.1522 g, 1 mmol) was added to a stirred mixture of L-asparagine (0.1321 g, 1.0 mmol) and potassium hydroxide (0.0561 g, 1 mmol) in hot methanol. The resultant yellow solution was then stirred at 333 K for 1 h. Subsequently, an aqueous solution (2 mL) of vanadyl sulfate hydrate (0.2540 g, 1 mmol) was added dropwise and stirred for 2 h continuously. Finally, a methanol solution (5 mL) of 1,10-phenanthroline (0.1980 g, 1 mmol) was then added dropwise, and the mixture was stirred continuously for 3 h. The resultant solution was filtered and kept at room temperature, and reddish brown blocky crystals suitable for X-ray diffraction were obtained after several days. It was characterized by IR and single crystal X-ray diffraction. It crystallized in triclinic crystal system, P-1 space group with the cell parameters: a＝0.98990(10) nm, b＝1.21591(11) nm, c＝1.28349(12) nm, α＝66.8180(10)o, β＝83.816(2)o, γ＝66.4150(10)o, V＝1.2992(2) nm3, Dc＝1.430 g·cm-3, Z＝1, F(000)＝580, R1＝0.0626, wR2＝0.1631. The interactions of the complex with calf thymus DNA (CT-DNA) and bovine serum albumin (BSA) were carried out in 10 mmol·L-1 Tris-HCl/10 mmol·L-1 NaCl (pH 7.1) buffer solutions. In the experiment of interactions with CT-DNA, absorption titrations were carried out by using a fixed complex concentration to which increments of DNA stock solutions were added. The complex-DNA solutions were incubated for 2 h before the absorption spectra in the 150～250 nm wavelength range were recorded. For fluorescence experiments, the complex solution was added to the fixed concentration CT-DNA solutions treated with ethidium bromide. The emission spectra was recorded range from 535 to 675 nm at the excitation wavelength of 258 nm. Circular dichroism (CD) spectra were measured with a quartz cell of 1 cm path length after the increasing concentration of complex was added to the fixed concentration CT-DNA solutions for 2 h. Each sample solution was scanned in the range of 220～320 nm with a scan speed of 100 nm·min-1 and 1 s response time. Viscosities of the DNA-complex system were measured at (30.0±0.1) ℃ using an Ubbelodhe viscometer. The results indicate that the complex binds to CT-DNA with a weak intercalative mode. The binding constant Kb obtained from absorption spectra was 2.17×103 L·mol-1, and the linear Stern-Volmer quenching constant Ksq obtained from fluorescence spectra was 1.44. Meanwhile, the interactions of the complex with BSA have also been studied by spectroscopy. The results indicate that the complex can markedly quench the intrinsic fluorescence of BSA via a static quenching process, and cause its conformational change. The calculated apparent binding constant Kb was 8.9×104 and the binding site number n was 1.04.

Key words： oxovanadium complex; L-asparagine schiff base; crystal structure; DNA; bovine serum albumin (BSA)

参考文献

[1] Takeuchi, K. J.; Samuels, G. J.; Gillert, S. W. Inorg. Chem. 1983, 22, 1407.

[2] He, H.; Wang, L.-L.; Zhang, M.; Jiao, Q.-C.; Chuong, P.-H. Chin. Pharm. J. 2007, 42, 1287. (何华, 王羚郦, 张明, 焦庆才, Chuong, P.-H. 中国药学杂志, 2007, 42, 1287.)

[3] Wang, Z.-Q.; Zhang, Z.-Q.; Yu, J.-H.; Ni, K.-Y.; He, H. Acta Chim. Sinica 2008, 66, 2693. (王志群, 张志强, 余江河, 倪坤仪, 何华, 化学学报, 2008, 66, 2693.)

[4] Kragh-Hansen, U. Pharmacol. Rev. 1981, 33, 17.

[5] Cszerháti, T.; Forgács, E. J. Chromatogr. A 1995, 699, 285.

[6] Dubyak, G. R.; Kleinzeller, A. J. Biol. Chem. 1980, 255, 5306.

[7] Ghosh, P.; D’Cruz, O. J.; Narla, R. K.; Uckum, F. M. Clin. Cancer Res. 2000, 6, 1536.

[8] Evangelou, A.; Karkabounas, S.; Kalpouzos, G.; Malamas, M.; Liasko, R.; Stefanou, D.; Vlahos, A. T.; Kabanos, T. A. Cancer Lett. 1997, 119, 221.

[9] Ghosh, P.; Ghosh, S.; D’Cruz, O. J.; Uckum, F. M. J. Inorg. Biochem. 1998, 72, 89.

[10] Krejsa, C. M.; Nadler, S. G.; Esselstyn, J. M.; Kavanagh, T. J.; Ledbetter, J. A.; Schieven, G. L. J. Bio1. Chem. 1997. 272, 11541.

[11] Nath, M.; Patra, A. K.; Chakravarty, A. R. J. Inorg. Biochem. 2005, 99, 2062.

[12] Evangelou, A. M. Crit. Rev. Oncol. Hemat. 2002, 42, 249.

[13] Djordjevic, C.; Wampler, G. L. J. Inorg. Biochem. 1985, 25, 51.

[14] Sasmal, P. K.; Patra, A. K.; Chakravarty, A. R. J. Inorg. Biochem. 2008, 102, 1463.

[15] Heater, S. J.; Carrano, M. W.; Rains, D.; Walter, R.; Ji, D.; Yan, Q.; Czernuszewicz, R. S.; Carrano, C. J. Inorg. Chem. 2000, 39, 3881.

[16] Kwong, D. W. J.; Chan, O. Y.; Shek, L. K.; Wong, R. N. S. J. Inorg. Biochem. 2005, 99, 2062.

[17] Li, L.-Z.; Guo, Z.-H.; Zhang, Q.-F.; Xu, T.; Wang, D.-Q. Inorg. Chem. Commun. 2010, 13, 1166.

[18] Xu, T.; Li, L.-Z.; Zhou, S.-F.; Guo, G.-Q.; Niu, M.-J. J. Chem. Crystallogr. 2005, 35, 263.

[19] Li L.-Z.; Xu, T.; Wang, D.-Q.; Ji, H.-W. Chin. J. Inorg. Chem. 2004, 20, 236. (李连之, 许涛, 王大奇, 冀海伟, 无机化学学报, 2004, 20, 236.)

[20] Bian, L.; Li, L.-Z.; Zhang, Q.-F.; Liu, H.-L.; Wang, D.-Q. Acta Chim. Sinica 2011, 69, 1661. (边琳, 李连之, 张庆富, 刘后炉, 王大奇, 化学学报, 2011, 69, 1661.)

[21] Kenji, K.; Makoto, T.; Ken, H.; Naohisa, Y.; Yoshitane, K. Inorg. Chim. Acta 2000, 305, 172.

[22] Long, E. C.; Barton, J. K. Acc. Chem. Res. 1990, 23, 271.

[23] Tysoe, S. A.; Morgan, R. J.; Baker, A. D.; Strekas, T. C. J. Phys. Chem. 1993, 97, 1707.

[24] Lakowicz, J. R.; Weber, G. Biochemistry 1973, 12, 4161.

[25] Zhong, W.-T.; Wu, J.-Z. Chin. J. Inorg. Chem. 2003, 19, 196. (钟文添, 吴建中, 无机化学学报, 2003, 19, 196.)

[26] Wolfe, A.; Shimer, G. H.; Meehan, T. Biochemistry 1987, 26, 6392.

[27] Strothkamp, K. G.; Strothkamp, R. E. J. Chem. Educ. 1994, 71, 77.

[28] Pu, X.-W.; Li, L.-Z.; Dong, J.-F.; Huang, L.; Bian, L. Acta Chim. Sinica 2011, 69, 647. (蒲雪炜, 李连之, 董建方, 黄蕾, 边琳, 化学学报, 2011, 69, 647.)

[29] Dong, J.-F.; Li, L.-Z.; Liu, G.-H.; Xu, T.; Wang, D.-Q. J. Mol. Struct. 2011, 986, 57.

[30] Li, J.-H.; Dong, J.-F.; Cui, H.; Xu, T.; Li, L.-Z. Transition Met. Chem. 2012, 37, 175.

[31] Mansuri, T. H.; Mital, R.; Srivastava, T. S.; Parekh, H.; Chitnis, M. P. J. Inorg. Biochem. 1991, 44, 239.

[32] Lakowicz, J. R.; Weber, G. Biochemistry 1973, 12, 4161.

[33] Li, Y.-P.; Wu, Y.-B.; Zhao, J.; Yang, P. J. Inorg. Biochem. 2007, 101, 283.

[34] Uma, V.; Kanthimathi, M.; Weyhermuller, T.; Nair, B. U. J. Inorg. Biochem. 2005, 99, 2299.

[35] Lincoln, P.; Tuite, E.; Norden, B. J. Am. Chem. Soc. 1997, 119, 1454.

[36] Satyanarayana, S.; Dabrowiak, J. C.; Chaires, J. B. Biochemistry 1993, 32, 2573.

[37] Guo, X. J. Experimental Technology of Fluorescence and Its Application in Molecular Biology, Science Press, Bejing, 1979, p. 123. (郭小君, 荧光实验技术及其在生物化学中的应用, 科学出版社, 北京, 1979, p. 123.)

[38] Toneatto, J.; Argüello, G. A. J. Inorg. Biochem. 2011, 105, 645.

[39] Lakowicz, J. R.; Weber, G. Biochemistry 1973, 12, 4161.

[40] Hu, Y.-J.; Liu, Y.; Wang, J.-B.; Xiao, X.-H.; Qu, S.-S. J. Pharm. Biomed. Anal. 2004, 36, 915.

[41] Peter, T. Adv. Protein Chem. 1985, 37, 161.

[42] Sulkowska, A. J. Mol. Struct. 2002, 614, 227.

[43] Wang, Y.-Q.; Zhang, H.-M.; Zhang, G.-C.; Tao, W.-H.; Fei, Z.-H.; Liu, Z.-T. J. Pharm. Biomed. Anal. 2007, 43, 1869.

[44] Tysoe, S. A.; Morgan, R. J.; Baker, A. D.; Strekas, T. C. J. Phys. Chem. 1993, 97, 1707.

[45] Ran, D.-H.; Wu, X.; Zheng, J.-H.; Yang, J.-H.; Zhou, H.-P.; Zhang, M.-F.; Tang, Y.-J. J. Fluoresc. 2007, 17, 721.

[46] Hu, Y.-J.; Liu, Y.; Wang, J.-B.; Xiao, X.-H.; Qu, S.-S. J. Pharm. Biomed. 2004, 36, 915.

[47] Liu, J.-Q.; Tian, J.-N.; He, W.-Y.; Xie, J.-P.; Hu, Z.-D.; Chen, X.-G. J. Pharm. Biomed. Anal. 2004, 35, 671. Sheldrick, G. M. SHELXTL 6. 10, Bruker Analytical Instrumentation, Madison, Wisconsin, USA, 2000.
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