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Influence of Taxifolin on the Human Serum Albumin–Propranolol Interaction: Multiple Spectroscopic and Chemometrics Investigations and Molecular Dynamics Simulation

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Abstract

The aim of the present study is to characterize the competition between propranolol (PROP) and taxifolin (TAX) in binding to human serum albumin (HSA) in a physiological buffer (pH 7.4) using multiple spectroscopic, chemometrics and molecular dynamics simulation measurements. Fluorescence analysis was used to determine the binding and quenching properties of HSA–ligand complexes in binary and ternary systems. These spectral data were further analyzed by the multivariate curve resolution-alternating least squares method. In addition, the concentration profiles and pure spectra of three species (HSA, ligand and HSA–ligand complex) and the apparent equilibrium constants K app were evaluated. Fluorescence spectroscopy showed that in the presence of TAX, the binding constant of HSA–PROP increased. The effect of ligands on the secondary structure of the protein has been analyzed by using Fourier transform infrared spectra. The conformational change of the protein was analyzed using synchronous fluorescence spectroscopy, three-dimensional fluorescence spectra and molecular dynamics (MD) simulation. The results of synchronous fluorescence and three-dimensional fluorescence spectra show that PROP alters the microenvironment around the tryptophan (Trp) and tyrosine (Tyr) residues in the presence of TAX. According to the MD simulation, these ligands can interact with the protein, affecting the secondary structure of HSA and modifying its tertiary structure. MD simulations and experimental data support each other.

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References

  1. Huang, B.X., Kim, H.Y., Dass, C.: Probing three-dimensional structure of bovine serum albumin by chemical cross-linking and mass spectrometry. J. Am. Soc. Mass Spectr. 15, 1237–1247 (2004)

    Article  CAS  Google Scholar 

  2. Martini, S., Bonechi, C., Rossi, C.: Interaction between vine pesticides and bovine serum albumin studied by nuclear spin relaxation data. J. Agr. Food. Chem. 58, 10705–10709 (2010)

    Article  CAS  Google Scholar 

  3. Kalanur, S.S., Seetharamappa, J., Kalalbandi, V.K.L.: Characterization of interaction and the effect of carbamazepine on the structure of human serum albumin. J. Pharm. Biomed. Anal. 53, 660–666 (2010)

    Article  CAS  Google Scholar 

  4. Bourassa, P., Dubeau, S., Maharvi, GhM, Fauq, A.H., Thomas, T.J., TajmirRiahi, H.A.: Binding of antitumor tamoxifen and its metabolites 4-hydroxytamoxifen and endoxifen to human serum albumin. Biochimie 93, 1089–1101 (2011)

    Article  CAS  Google Scholar 

  5. Zhu, L., Yang, F., Chen, L., Meehan, E.J., Huang, M.: A new drug binding subsite on human serum albumin and drug–drug interaction studied by X-ray crystallography. J. Struct. Biol. 162, 40–49 (2008)

    Article  CAS  Google Scholar 

  6. Zohoorian-Abootorabi, T., Sanee, H., Iranfar, H., Saberi, M.R., Chamani, J.: Separate and simultaneous binding effects through a non-cooperative behavior between cyclophosphamide hydrochloride and fluoxymesterone upon interaction with human serum albumin: multi-spectroscopic and molecular modeling approaches. Spectrochim. Acta A 88, 177–191 (2012)

    Article  CAS  Google Scholar 

  7. Huang, X., Xiong, P., Xiong, C., Cai, Y., Wei, A., Wang, J., Liang, X., Ruan, J.: In vitro and in vivo antitumor activity of Macrothelypteris torresiana and its acute/subacute oral toxicity. Phytomedicine 17, 930–934 (2010)

    Article  CAS  Google Scholar 

  8. Wang, T., Xiang, B.R., Li, Y., Chen, C.Y., Zhou, X.H., Wang, Z.M., Dong, Y., Wan, Y., Fang, H.S.: Studies on the binding of a carditionic agent to human serum albumin by two-dimensional correlation fluorescence spectroscopy and molecular modeling. J. Mol. Struct. 921, 188–198 (2009)

    Article  CAS  Google Scholar 

  9. Anzenbacher, P., Zanger, U.M.: Metabolism of drugs and other xenobiotics. Wiley Online Library, New York (2012)

    Book  Google Scholar 

  10. Papadopoulou, A., Green, R.J., Frazier, R.A.: Interaction of flavonoids with bovine serum albumin: a fluorescence quenching study. J. Agr. Food Chem. 53, 158–163 (2005)

    Article  CAS  Google Scholar 

  11. Shi, S., Zhang, Y., Xiong, X., Huang, K., Chen, X., Peng, M.: The influence of flavonoids on the binding of pantoprazole to bovine serum albumin by spectroscopic methods: with the viewpoint of food/drug interference. Food Chem. 135, 1083–1090 (2012)

    Article  CAS  Google Scholar 

  12. Yang, Y., Hu, Q., Fan, Y., Shen, H.: Study on the binding of luteolin to bovine serum albumin. Spectrochim. Acta A 69, 432–436 (2008)

    Article  Google Scholar 

  13. Gotardo, M.A., Tognolli, J.O., Pezza, H.R., Pezza, L.: Detection of propranolol in pharmaceutical formulations by diffuse reflectance spectroscopy. Spectrochim. Acta A 69, 1103–1109 (2008)

    Article  Google Scholar 

  14. Li, H.M., Hu, Y.Z.: Spectroscopic investigation of inner filter effect by magnolol solutions. Spectrochim. Acta A 68, 1263–1268 (2007)

    Article  Google Scholar 

  15. Shi, X., Li, X., Sun, Y., Wei, W., Yang, R., Zhang, H., Jin, Y.: In vitro study of the binding of taxifolin to bovine serum albumin and the influence of common ions on the binding. J. Solution Chem. 39, 482–494 (2010)

    Article  CAS  Google Scholar 

  16. Madrakian, T., Afkhami, A., Mohammadnejad, M.: Simultaneous spectrofluorimetric determination of levodopa and propranolol in urine using feed-forward neural networks assisted by principal component analysis. Talanta 78, 1051–1055 (2009)

    Article  CAS  Google Scholar 

  17. Lackowicz, J.R.: Principles of Fluorescence Spectroscopy, pp. 111–150. Plenum Press, New York (1983)

    Book  Google Scholar 

  18. de Juan, A., Tauler, R.: Chemometrics applied to unravel multicomponent processes and mixtures revisiting latest trends in multivariate resolution. Anal. Chim. Acta 500, 195–210 (2003)

    Article  Google Scholar 

  19. Zachariassen, C.B., Larsen, J., van den Berg, F., Bro, R., de Juan, A., Tauler, R.: Comparison of PARAFAC2 and MCR-ALS for resolution of an analytical liquid dilution system. Chemom. Intell. Lab. Syst. 83, 13–25 (2006)

    Article  CAS  Google Scholar 

  20. Maeder, M.: Evolving factor analysis for the resolution of overlapping chromatographic peaks. Anal. Chem. 59, 527–530 (1987)

    Article  CAS  Google Scholar 

  21. Golub, G.H., van Loan, C.F.: Matrix Computations, 2nd edn. John Hopkins University Press, Baltimore (1989)

    Google Scholar 

  22. Tauler, R., Smilde, A., Kowalski, B.: Selactivity, local rank, three-way data analysis and ambiguity in multivariant curve resolution. J. Chemom. 9, 31–58 (1995)

    Article  CAS  Google Scholar 

  23. Lindahl, E., Hess, B., Van Der Spoel, D.: GROMACS 3.0: a package for molecular simulation and trajectory analysis. J. Mol. Model. 7, 306–317 (2001)

    CAS  Google Scholar 

  24. Díaz-Vergara, N., Piñeiro, Á.: Molecular dynamics study of triosephosphate isomerase from Trypanosoma cruzi in water/decane mixtures. J. Phys. Chem. B 112, 3529–3539 (2008)

    Article  Google Scholar 

  25. Micaêlo, N.M., Soares, C.M.: Protein structure and dynamics in ionic liquids. Insights from molecular dynamics simulation studies. J. Phys. Chem. B 112, 2566–2572 (2008)

    Article  Google Scholar 

  26. Todorova, N., Legge, F.S., Treutlein, H., Yarovsky, I.: Systematic comparison of empirical forcefields for molecular dynamic simulation of insulin. J. Phys. Chem. B 112, 11137–11146 (2008)

    Article  CAS  Google Scholar 

  27. Schuttelkopf, A.W., Van Aalten, D.M.: PRODRG: a tool for high-throughput crystallography of protein–ligand complexes. Acta Crystallogr. D 60, 1355–1363 (2004)

    Article  Google Scholar 

  28. Schmidt, M.W., Baldridge, K.K., Boatz, J.A., Elbert, S.T., Gordon, M.S., Jensen, J.H., Koseki, S., Matsunaga, N., Nguyen, K.A., Su, S.: General atomic and molecular electronic structure system. J. Comput. Chem. 14, 1347–1363 (1993)

    Article  CAS  Google Scholar 

  29. Hess, B., Bekker, H., Berendsen, H.J., Fraaije, J.G.: LINCS: a linear constraint solver for molecular simulations. J. Comput. Chem. 18, 1463–1472 (1997)

    Article  CAS  Google Scholar 

  30. Darden, T., York, D., Pedersen, L.: Particle mesh Ewald: an N·log (N) method for Ewald sums in large systems. J. Chem. Phys. 98, 10089–10092 (1993)

    Article  CAS  Google Scholar 

  31. Berendsen, H.J., Postma, J.P.M., van Gunsteren, W.F., DiNola, A., Haak, J.: Molecular dynamics with coupling to an external bath. J. Chem. Phys. 81, 3684–3690 (1984)

    Article  CAS  Google Scholar 

  32. Danciulescu, C., Nick, B., Wortmann, F.J.: Structural stability of wild type and mutated α-keratin fragments: molecular dynamics and free energy calculations. Biomacromolecules 5, 2165–2175 (2004)

    Article  CAS  Google Scholar 

  33. Chamani, J., Tafrishi, N., Momen-Heravi, M.: Characterization of the interaction between human lactoferrin and lomefloxacin at physiological condition: multi-spectroscopic and modeling description. J. Lumin. 130, 1160–1168 (2010)

    Article  CAS  Google Scholar 

  34. Lakowicz, J.: Principles of Fluorescence Spectroscopy. Springer, New York (2006)

    Book  Google Scholar 

  35. Qin, P., Liu, R., Pan, X., Fang, X., Mou, Y.: Impact of carbon chain length on binding of perfluoroalkyl acids to bovine serum albumin determined by spectroscopic methods. J. Agr. Food Chem. 58, 5561–5567 (2010)

    Article  CAS  Google Scholar 

  36. Yue, Y., Chen, X., Qin, J., Yao, X.: A study of the binding of CI Direct Yellow 9 to human serum albumin using optical spectroscopy and molecular modeling. Dyes Pigments 79, 176–182 (2008)

    Article  CAS  Google Scholar 

  37. Housaindokht, M.R., Rouhbakhsh Zaeri, Z., Bahrololoom, M., Chamani, J., Bozorgmehr, M.R.: Investigation of the behavior of HSA upon binding to amlodipine and propranolol: spectroscopic and molecular modeling approaches. Spectrochim. Acta A 85, 79–84 (2012)

    Article  CAS  Google Scholar 

  38. Subramanyam, R., Gollapudi, A., Bonigala, P., Chinnaboina, M., Amooru, D.G.: Betulinic acid binding to human serum albumin: a study of protein conformation and binding affinity. J. Photoch. Photobio. B 94, 8–12 (2009)

    Article  CAS  Google Scholar 

  39. Mohseni-Shahri, F.S., Housaindokht, M.R., Bozorgmehr, M.R., Moosavi-Movahedi, A.A.: The influence of theflavonoid quercetin on the interaction of propranolol with human serum albumin: experimental and theoretical approaches. J. Lumin. 154, 229–240 (2014)

    Article  CAS  Google Scholar 

  40. Zhang, G., Que, Q., Pan, J., Guo, J.: Study of the interaction between icariin and human serum albumin by fluorescence spectroscopy. J. Mol. Struct. 881, 132–138 (2008)

    Article  CAS  Google Scholar 

  41. Yang, L., Huo, D., Hou, C., Yang, M., Fa, H., Luo, X.: Interaction of monosulfonate tetraphenyl porphyrin (H2TPPS1) with plant-esterase: determination of the binding mechanism by spectroscopic methods. Spectrochim. Acta A 78, 1349–1355 (2011)

    Article  Google Scholar 

  42. Abdollahpour, N., Asoodeh, A., Saberi, M.R., Chamani, J.: Separate and simultaneous binding effects of aspirin and amlodipine to human serum albumin based on fluorescence spectroscopic and molecular modeling characterizations: a mechanistic insight for determining usage drugs doses. J. Lumin. 131, 1885–1899 (2011)

    Article  CAS  Google Scholar 

  43. He, L., Wang, X., Liu, B., Wang, J., Sun, Y., Gao, E., Xu, S.: Study on the interaction between promethazine hydrochloride and bovine serum albumin by fluorescence spectroscopy. J. Lumin. 131, 285–290 (2011)

    Article  CAS  Google Scholar 

  44. Caruso, Í.P., Vilegas, W., de Souza, F.P., Fossey, M.A., Cornélio, M.L.: Binding of antioxidant flavone isovitexin to human serum albumin investigated by experimental and computational assays. J. Pharmaceut. Biomed. 98, 100–106 (2014)

    Article  CAS  Google Scholar 

  45. Zhang, Y.Z., Zhou, B., Zhang, X.P., Huang, P., Li, C.H., Liu, Y.: Interaction of malachite green with bovine serum albumin: determination of the binding mechanism and binding site by spectroscopic methods. J. Hazard. Mater. 163, 1345–1352 (2009)

    Article  CAS  Google Scholar 

  46. Rahmelow, K., Hubner, W.: Secondary structure determination of proteins in aqueous solution by infrared spectroscopy: a comparison of multivariate data analysis methods. Anal. Biochem. 241, 5–13 (1996)

    Article  CAS  Google Scholar 

  47. Jung, C.: Insight into protein structure and protein–ligand recognition by Fourier transform infrared spectroscopy. J. Mol. Recognit. 13, 325–351 (2000)

    Article  CAS  Google Scholar 

  48. Housaindokht, M.R., Bozorgmehr, M.R., Bahrololoom, M.: Analysis of ligand binding to proteins using molecular dynamics simulations. J. Theor. Biol. 254, 294–300 (2008)

    Article  CAS  Google Scholar 

  49. Vassura, M., Margara, L., Di Lena, P., Medri, F., Fariselli, P., Casadio, R.: FT-COMAR: fault tolerant three-dimensional structure reconstruction from protein contact maps. Bioinformatics 24, 1313–1315 (2008)

    Article  CAS  Google Scholar 

  50. Ding, F., Diao, J.X., Sun, Y., Sun, Y.: Bioevaluation of human serum albumin–hesperidin bioconjugate: insight into protein vector function and conformation. J. Agr. Food Chem. 60, 7218–7228 (2012)

    Article  CAS  Google Scholar 

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Acknowledgments

The financial support for this work was provided by Research Council of Ferdowsi University of Mashhad (Research Project No. 3/24357-91/10/12).

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Authors and Affiliations

  1. Department of Chemistry, Faculty of Science, Ferdowsi University of Mashhad, Mashhad, Iran

    Fatemeh Sadat Mohseni-Shahri & Mohammad Reza Housaindokht

  2. Department of Chemistry, Mashhad Branch, Islamic Azad University, Mashhad, Iran

    Mohammad Reza Bozorgmehr

  3. Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran

    Ali Akbar Moosavi-Movahedi

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  1. Fatemeh Sadat Mohseni-Shahri
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  2. Mohammad Reza Housaindokht
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  3. Mohammad Reza Bozorgmehr
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Correspondence to Fatemeh Sadat Mohseni-Shahri or Mohammad Reza Housaindokht.

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Mohseni-Shahri, F.S., Housaindokht, M.R., Bozorgmehr, M.R. et al. Influence of Taxifolin on the Human Serum Albumin–Propranolol Interaction: Multiple Spectroscopic and Chemometrics Investigations and Molecular Dynamics Simulation. J Solution Chem 45, 265–285 (2016). https://doi.org/10.1007/s10953-016-0435-4

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