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Biophysical Studies on the Site-Selective Binding of a Synthesized Selenium–Quercetin Complex on a Protein

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Abstract

A selenium–quercetin complex (SEQC) was synthesized and its structure was identified by IR, LC-MS and 1H-NMR. Its biochemical effects on bovine serum albumin (BSA) were studied by measuring its molecular spectra including three-dimensional fluorescence, ultraviolet and circular dichroism (CD) spectra. The interaction of SEQC and BSA is discussed in terns of fluorescence quenching and Förster’s non-radiation energy transfer theory. The thermodynamic parameters \(\Delta H^{\uptheta}\), \(\Delta G^{\uptheta}\), and \(\Delta S^{\uptheta}\) were calculated at different temperatures and the results indicate that the interaction is an endothermic as well as an entropy generating process. The binding site was explored by the fluorescence probe technique using warfarin and ibuprofen as markers. It was found that around body temperature hydrophobic forces maintained the average distance from the tryptophan residue in domain II of BSA (donor) to SEQC (acceptor) at 3.76 nm. The conformational changes of BSA were investigated by three-dimensional fluorescence and circular dichroism spectra.

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References

  1. Balasubramanian, R., Narayanan, M., Kedalgovindaram, L., Devarakonda Rama, K.: Cytotoxic activity of flavone glycoside from the stem of Indigofera aspalathoides Vahl. J. Nat. Med. 61(1), 80–83 (2007)

    Article  CAS  Google Scholar 

  2. Mavel, S., Dikic, B., Palakas, S., Emond, P., Greguric, I., de Gracia, A.G., Mattner, F., Garrigos, M., Guilloteau, D., Katsifis, A.: Synthesis and biological evaluation of a series of flavone derivatives as potential radioligands for imaging the multidrug resistance-associated protein 1 (ABCC1/MRP1). Bioorg. Med. Chem. 14, 1599–1607 (2006)

    Article  CAS  Google Scholar 

  3. Ronai, Z., Tillotson, J.K., Traganos, F., Darzynkiewicz, Z., Conaway, C.C., Clifford, C., Upadhyaya, P., El-Bayoumy, K.: Effects of organic and inorganic selenium compounds on rat mammary tumor cells. Int. J. Cancer 63, 428–434 (1995)

    Article  CAS  Google Scholar 

  4. Zhou, J., Wang, L.F., Wang, J.Y., Tang, N.: Antioxidative and anti-tumour activities of solid quercetin metal(II) complexes. Transit. Metal Chem. 26, 57–63 (2001)

    Article  CAS  Google Scholar 

  5. Zhang, H.X., Huang, X., Zhang, M.: Spectral diagnostics of the interaction between pyridoxine hydrochloride and bovine serum albumin in vitro. Mol. Biol. Rep. 35, 699–705 (2008)

    Article  CAS  Google Scholar 

  6. Stryer, L.: Fluorescence spectroscopy of proteins. Science 162, 526–533 (1968)

    Article  CAS  Google Scholar 

  7. Lakowicz, J.R.: Principles of Fluorescence Spectroscopy, 3rd edn. Springer, New York (2006)

    Book  Google Scholar 

  8. Ashoka, S., Seetharamappa, J., Kandagal, P.B., Shaikh, S.M.T.: Investigation of the interaction between trazodone hydrochloride and bovine serum albumin. J. Lumin. 121, 179–186 (2006)

    Article  CAS  Google Scholar 

  9. Lehrer, S.S.: Solute perturbation of protein fluorescence. The quenching of the tryptophyl fluorescence of model compounds and of lysozyme by iodide ion. Biochemistry 10, 3254–3263 (1971)

    Article  CAS  Google Scholar 

  10. Hu, Y.J., Yang, Y.O., Bai, A.M., Li, W., Liu, Y.: Investigation of the interaction between ofloxacin and bovine serum albumin: spectroscopic approach. J. Solution Chem. 3, 709–717 (2010)

    Article  Google Scholar 

  11. Ross, D.P., Subramanian, S.: Thermodynamics of protein association reactions: forces contributing to stability. Biochemistry 20, 3096–3102 (1981)

    Article  CAS  Google Scholar 

  12. Bhattacharya, A.A., Grune, T., Curry, S.: Crystallographic analysis reveals modes of binding of medium and long chain fatty acids to human serum albumin. J. Mol. Biol. 303, 721–732 (2000)

    Article  CAS  Google Scholar 

  13. Sulkowska, A.: Interaction of drugs with bovine serum and human serum albumin. J. Mol. Struct. 614, 227–232 (2002)

    Article  CAS  Google Scholar 

  14. Carter, D.C., Ho, J.X.: The structure of serum albumin. Adv. Protein Chem. 45, 153–203 (1994)

    Article  CAS  Google Scholar 

  15. Förster, T.: Intermolecular energy migration and fluorescence. Ann. Phys. 437, 55–75 (1948)

    Article  Google Scholar 

  16. Kamat, B.P.: Study of the interaction between fluoroquinolones and bovine serum albumin. J. Pharm. Biomed. Anal. 39, 1046–1050 (2005)

    Article  CAS  Google Scholar 

  17. Zhang, H.X., Mei, P., Yang, X.X.: Optical, structural and thermodynamic properties of the interaction between tradimefon and serum albumin. Spectrochim. Acta, Part A: Mol. Biomol. Spectrosc. 72, 621–626 (2009)

    Article  Google Scholar 

  18. Dufour, C., Dangles, O.: Flavonoid–serum albumin complexation: determination of binding constants and binding sites by fluorescence spectroscopy. Biochim. Biophys. Acta 1721, 164–173 (2005)

    Article  CAS  Google Scholar 

  19. Vaughan, W.M., Weber, G.: Oxygen quenching of pyrenebutyric acid fluorescence in water: a dynamic probe of the microenvironment. Biochemistry 9, 464–473 (1970)

    Article  CAS  Google Scholar 

  20. Shaikh, S.M.T., Seetharamappa, J., Ashoka, S., Kandaga, P.B.: A study of the interaction between bromopyrogallol red and bovine serum albumin by spectroscopic methods. Dyes Pigm. 73, 211–216 (2007)

    Article  CAS  Google Scholar 

  21. Rogers, D.M., Hirst, J.D.: First-principles calculations of protein circular dichroism in the near ultraviolet. Biochemistry 43, 11092–11102 (2004)

    Article  CAS  Google Scholar 

  22. Maiti, T.K., Ghosh, K.S., Debnath, J., Dasgupta, S.: Binding of all trans retinoic acid to human serum albumin: fluorescence FT-IR and circular dichroism studies. Int. J. Biol. Macromol. 38, 197–202 (2006)

    Article  CAS  Google Scholar 

  23. Zhang, H.X., Mei, P.: In vitro binding of furadan to bovine serum albumin. J. Solution Chem. 38, 351–361 (2009)

    Article  Google Scholar 

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Acknowledgements

The authors gratefully acknowledge the fund support of the Science and Technology Research Program of the Education Department, Hubei, China (Grant No. B20104301) and Scientific Research Project of Jingchu University of Technology (Grants No. ZR201108 and ZR201014).

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  1. College of Chemical and Pharmaceutical Engineering, Jingchu University of Technology, Jingmen, Hubei, 448000, People’s Republic of China

    Hua-xin Zhang & Kong-sai Chen

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  1. Hua-xin Zhang
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Correspondence to Hua-xin Zhang.

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Zhang, Hx., Chen, Ks. Biophysical Studies on the Site-Selective Binding of a Synthesized Selenium–Quercetin Complex on a Protein. J Solution Chem 41, 915–925 (2012). https://doi.org/10.1007/s10953-012-9844-1

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  • DOI: https://doi.org/10.1007/s10953-012-9844-1

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