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Binding Effect of Common Ions to Human Serum Albumin in the Presence of Norfloxacin: Investigation with Spectroscopic and Zeta Potential Approaches

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Abstract

In this work, the toxic influence of metallic ions (Al3+, Cu2+, Mg2+, Pb2+) on human serum albumin (HSA) in the absence and presence of norfloxacin (NRF) was studied by spectroscopic approaches [fluorescence quenching, synchronous fluorescence, three-dimensional fluorescence, circular dichroism, resonance light scattering (RLS) and zeta potential techniques] under simulated physiological conditions. Fluorescence spectroscopy revealed that these metallic ions and NRF can quench the HSA fluorescence, and this quenching effect became more significant when both ion and drug are present together. The binding constants and binding sites of metal ions with HSA in the absence and presence of NRF were determined, based on the fluorescence quenching results. Ion aggregation gives rise to an enhancement of the RLS intensity for HSA and the critical induced aggregation concentration (C CIAC) of the ions, causing HSA aggregation for binary and ternary systems. The zeta potential measurements indicate a combination of electrostatic and hydrophobic interactions between ion, NRF and HSA and the formed micelle-like clusters. These data illustrated that NRF has an effect on the interaction between HSA and metal ions, with relevance for various toxicological and therapeutic processes.

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References

  1. Zhang, H., Liu, R., Chi, Z., Gao, C.: Toxic effects of different charged metal ions on the target-bovine serum albumin. Spectrochim. Acta A 78, 523–527 (2011)

    Article  Google Scholar 

  2. Huang, K.S., Bayley, H., Liao, M.J., London, E., Khoran, H.G.: Refolding of an integral membrane protein. Denaturation, renaturation, and reconstitution of intact bacteriorhodopsin and two proteolytic fragments. J. Biol. Chem. 256, 3802–3809 (1981)

    CAS  Google Scholar 

  3. Brandts, J.F., Halvorson, H.R., Brennan, M.: Consideration of the possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residues. J. Biol. Chem. 14, 4953–4963 (1975)

    CAS  Google Scholar 

  4. Zamber, C.P., Lamba, J.K., Yasuda, K., Farnum, J., Thummel, K., Schuetz, J.D., Schuetz, E.G.: Natural allelic variants of breast cancer resistance protein (BCRP) and their relationship to BCRP expression in human intestine. Pharmacogenomics J. 13, 19–28 (2003)

    CAS  Google Scholar 

  5. Liotta, L., Espina, V., Mehta, A., Calvert, V., Rosenblatt, K., Geho, D., Munson, P., Young, L., Wulfkuhle, J., Petricoin, E.: Protein microarrays: meeting analytical challenges for clinical applications. Cancer Cell 3, 317–325 (2003)

    Article  CAS  Google Scholar 

  6. Wang, L., Liu, R.T., Chi, Z., Yang, B., Zhang, P., Wang, M.: Spectroscopic investigation on the toxic interactions of Ni(2+) with bovine hemoglobin. Spectrochim. Acta A 76, 155–160 (2010)

    Article  Google Scholar 

  7. Versieck, J.H.J., Barbier, F., Steyaert, H., De Rudder, J., Michels, H.: Determination of chromium and cobalt in human serum by neutron activation analysis. Clin. Chem. 24, 303–308 (1978)

    CAS  Google Scholar 

  8. Ohyoshi, E., Nakata, K., Kohata, S.: The interaction between human and bovine serum albumin and zinc studied by a competitive spectrophotometry. J. Inorg. Biochem. 75, 213–218 (1999)

    Article  CAS  Google Scholar 

  9. Cui, F., Kong, X., Qin, L., Zhang, G., Liu, Q., Lei, B., Yao, X.: Specific interaction of 40-O (a-l-cladinosyl) daunorubicin with human serum albumin: the binding site II on HSA molecular using spectroscopy and modelling. J. Photochem. Photobiol. B 95, 162–169 (2009)

    Article  CAS  Google Scholar 

  10. Kumar, C.V., Buranaprapuk, A.: Site-specific photocleavage of proteins. Angew. Chem. Int. Ed. Engl. 36, 2085–2087 (1997)

    Article  CAS  Google Scholar 

  11. Colmenarejo, G.: In silico prediction of drug-binding strengths to human serum albumin. Med. Res. Rev. 23, 275–301 (2003)

    Article  CAS  Google Scholar 

  12. Sugiol, S., Kashima, A., Mochizuki, S., Noda, M., Kobayashi, K.: Crystal structure of human serum albumin at 2.5 nm resolution. Protein Eng. 12, 439–446 (1999)

    Article  Google Scholar 

  13. Molla, A., Vasavanonda, S., Kumar, G., Sham, H.L., Johnson, M., Grabowski, B., Denissen, J.F., Kohlbrenner, W., Plattner, J.J., Leonard, J.M., Norbeck, D.W., Kempf, D.J.: Human serum attenuates the activity of protease inhibitors toward wild-type and mutant human immunodeficiency virus. Virology 250, 255–262 (1998)

    Article  CAS  Google Scholar 

  14. Tang, J.H., Qi, S.D., Chen, X.G.: Spectroscopic studies of the interaction of anticoagulant rodenticide diphacinone with human serum albumin. J. Mol. Struct. 779, 87–95 (2005)

    Article  CAS  Google Scholar 

  15. Sudlow, G., Birkett, D.J., Wade, D.N.: The characterization of two specific drug binding sites on human serum albumin. J. Mol. Pharmacol. 11, 824–832 (1975)

    CAS  Google Scholar 

  16. Curry, S., Mandelkow, H., Brick, P., Franks, N.: Crystal structure of human serum albumin complexed with fatty acid reveals an asymmetric distribution of binding sites. Nat. Struct. Biol. 5, 827–835 (1998)

    Article  CAS  Google Scholar 

  17. Krishnakumar, S.S., Panda, D.: Spatial relationship between the prodan site, Trp-214, and Cys-34 residues in human serum albumin and loss of structure through incremental unfolding. Biochemistry 41, 7443–7452 (2002)

    Article  CAS  Google Scholar 

  18. Swanson, B., Boppana, V., Vlasses, P., Rotmen, H., Ferguson, R.: Norfloxacin disposition after sequentially increasing oral doses. Antimicrob. Agents Chemother. 23, 284–288 (1983)

    Article  CAS  Google Scholar 

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

    Article  CAS  Google Scholar 

  20. Chen, Z., Zhang, T., Han, Y., Zhu, L.: Resonance light scattering spectroscopy study of interaction between norfloxacin and calf thymus DNA and its analytical application. Spectrochim. Acta A 65, 919–924 (2006)

    Article  Google Scholar 

  21. Gurrieri, S., Aliffi, A., Bellacchio, E., Lauceri, R., Purrello, R.: Spectroscopic characterization of porphyrin supramolecular aggregates on poly-lysine and their application to quantitative DNA determination. Inorg. Chim. Acta 286, 121–128 (1999)

    Article  CAS  Google Scholar 

  22. Li, Z.P., Li, K.A., Tong, S.Y.: Determination for micro amounts of nucleic acids by a resonance light scattering technique with dequalinium chloride. Talanta 55, 669–674 (2001)

    Article  CAS  Google Scholar 

  23. Huang, C.Z., Li, K.A., Tong, S.Y.: Determination of nucleic acids by a resonance light-scattering technique with alpha, beta, gamma, delta-tetrakis [4(trimethylammoniumyl) phenyl] porphine. Anal. Chem. 68, 2259–2263 (1996)

    Article  CAS  Google Scholar 

  24. Jia, R.P., Dong, L.J., Li, Q.F., Chen, X.G., Hu, Z.D.: A highly sensitive assay for protein with dibromochloro–arsenazo–Al3+ using resonance light scattering technique and its application. Talanta 57, 693–699 (2002)

    Article  CAS  Google Scholar 

  25. Wang, F., Huang, W.: Determination of curcumin by its quenching effect on the fluorescence of Eu3+–tryptophan complex. J. Pharm. Biomed. Anal. 43, 393–398 (2007)

    Article  Google Scholar 

  26. Roessler, S., Zimmermann, R., Scharnweber, D., Werner, C., Worch, H.: Characterization of oxide layers on Ti6Al4V and titanium by streaming potential and streaming current measurements. Colloids Surf. B 26, 387–395 (2002)

    Article  CAS  Google Scholar 

  27. Krajewski, A., Malavolti, R., Piancastelli, A.: Albumin adhesion on some biological and non-biological glasses and connection with their ζ potentials. Biomaterials 17, 53–60 (1996)

    Article  CAS  Google Scholar 

  28. Vanapalli, S., Coupland, J.N.: Characterization of food colloids by phase analysis light scattering. Food Hydrocoll. 14, 315–317 (2000)

    Article  CAS  Google Scholar 

  29. Rezaei Behbehani, G., Tazikeh, E., Saboury, A.A., Divsalar, A., Monajjemi, M.: Thermodynamic study on the interaction of copper ion with human growth hormone. J. Solution Chem. 39, 153–164 (2010)

    Article  CAS  Google Scholar 

  30. Morel, M., Thomassin, M., Berthelot, A., Guillaume, Y.C., André, C.: Modelisation of the association mechanism of a series of huperzine derivatives used for Alzheimer disease with human serum albumin: effect of the magnesium cation. Chromatographia 61, 253–258 (2005)

    Article  CAS  Google Scholar 

  31. Long, X., Zhang, C., Cheng, J., Bi, S.: A novel method for study of the aggregation of protein induced by metal ion aluminium(III) using resonance Rayleigh scattering technique. Spectrochim. Acta A Mol. Biomol. Spectrosc. 69, 71–79 (2008)

    Article  Google Scholar 

  32. Liu, Q., Bei, Y., Zhou, F.: Removal of lead(II) from aqueous solution with amino-functionalized nanoscale zero-valent iron. Cent. Eur. J. Chem. 7, 79–82 (2009)

    Article  CAS  Google Scholar 

  33. Pan, H., Tao, X., Mao, C., Zhu, J.J., Liang, F.: Aminopolycarboxyl-modified Ag2S nanoparticles: synthesis, characterization and resonance light scattering sensing for bovine serum albumin. Talanta 71, 276–281 (2007)

    Article  CAS  Google Scholar 

  34. Chakrabarty, A., Mallick, A., Haldar, B., Das, P., Chattophadhyay, P.: Binding interaction of a biological photosensitizer with serum albumins: A biophysical study. Biomacromolecules 8, 920–927 (2007)

    Article  CAS  Google Scholar 

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

    Article  CAS  Google Scholar 

  36. Zucker, S.D., Goessling, W., Gollan, J.L.: Kinetics of bilirubin transfer between serum albumin and membrane vesicles. Insight into the mechanism of organic anion delivery to the hepatocyte plasma membrane. J. Biol. Chem. 270, 1074–1081 (1995)

    Article  CAS  Google Scholar 

  37. Ahmad, B., Parveen, S., Khan, R.H.: Effect of albumin conformation on the binding of ciprofloxacin to human serum albumin: A novel approach directly assigning binding site. Biomacromolecules 7, 1350–1356 (2006)

    Article  CAS  Google Scholar 

  38. Malhotra, A., Coupland, J.N.: The effect of surfactants on the solubility, zeta potential, and viscosity of soy protein isolates. Food Hydrocoll. 18, 101–108 (2004)

    Article  CAS  Google Scholar 

  39. Tantra, R., Schulze, P., Quincey, P.: Effect of nanoparticle concentration on zeta-potential measurement results and reproducibility. Particuology 8, 279–285 (2010)

    Article  CAS  Google Scholar 

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

    Article  CAS  Google Scholar 

  41. Jun Hu, Y., 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. 39, 709–717 (2010)

    Article  Google Scholar 

  42. Sulkowska, A., Bojko, B., Rownicka, J., Sulkowski, W.W.: Competition of drugs to serum albumin in combination therapy. J. Mol. Struct. 249, 792–793 (2006)

    Google Scholar 

  43. More, R.V., Mote, S.U., Patil, R.Sh., Kolekar, B.G.: Interaction between riboflavin and norfloxacin and analytical application in the determination of vitamin B2. J. Solution Chem. 39, 97–106 (2010)

    Article  CAS  Google Scholar 

  44. Lakowicz, J.R., Weber, G.: Quenching of fluorescence by oxygen. A probe for structural fluctuations in macromolecules. Biochemistry 12, 4161–4170 (1973)

    Article  CAS  Google Scholar 

  45. 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 

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

    Article  CAS  Google Scholar 

  47. Macia Zek Jurczyk, M., Sulkowska, A., Bojka, B., Rownicka, J., Sulkowski, W.W.: Fluorescence analysis of competition of phenylbutazone and methotrexate in binding to serum albumin in combination treatment in rheumatology. J. Mol. Struct. 881, 97–106 (2008)

    Article  Google Scholar 

  48. Pan, X., Liu, J., Zhang, D., Chen, X., Song, W., Wu, F.: Binding of dicamba to soluble and bound extracellular polymeric substances (EPS) from aerobic activated sludge: A fluorescence quenching study. J. Colloid Interface Sci. 345, 442–447 (2010)

    Article  CAS  Google Scholar 

  49. Lu, Y., Wang, G., Lu, X., Lv, J., Xu, M., Zhang, W.: Molecular mechanism of interaction between norfloxacin and trypsin studied by molecular spectroscopy and modelling. Spectrochim. Acta A 75, 261–266 (2010)

    Article  Google Scholar 

  50. Shen, X.C., Liou, X.Y., Ye, L.P., Liang, H., Wang, Z.Y.: Spectroscopic studies on the interaction between human hemoglobin and CdS quantum dots. J. Colloid Interface Sci. 311, 400–406 (2007)

    Article  CAS  Google Scholar 

  51. Wang, L.Y., Zhou, Y.Y., Wang, L.: Synchronous fluorescence determination of protein with functionalized CdS nanoparticles as a fluorescence probe. Anal. Chim. Acta 466, 87–92 (2002)

    Article  CAS  Google Scholar 

  52. Klajnert, B., Bryszewska, M.: Fluorescence studies on PAMAM dendrimers interactions with bovine serum albumin. Bioelectrochemistry 55, 33–35 (2002)

    Article  CAS  Google Scholar 

  53. Chi, Z., Liu, R., Yang, B., Zhang, H.: Toxic interaction mechanism between oxytetracycline and bovin hemoglobin. J. Hazard. Mater. 180, 741–747 (2010)

    Article  CAS  Google Scholar 

  54. 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 

  55. Ding, F., Han, B.Y., Liu, W., Zhang, L., Sun, Y.: Interaction of imidacloprid with hemoglobin by fluorescence and circular dichroism. J. Fluoresc. 20, 753–762 (2010)

    Article  CAS  Google Scholar 

  56. Sklar, L.A., Hudson, B.S., Simoni, R.D.: Conjugated polyene fatty acids as fluorescent probes: binding to bovine serum albumin. Biochemistry 16, 5100–5108 (1977)

    Article  CAS  Google Scholar 

  57. Cui, F.L., Fan, J., Li, J.P., Hu, Z.D.: Interactions between 1-benzoyl-4-p-chlorophenyl thiosemicarbazide and serum albumin: investigation by fluorescence spectroscopy. Bioorg. Med. Chem. 12, 151–157 (2004)

    Article  CAS  Google Scholar 

  58. Sanei, H., Asoodeh, A., Hamedakbari-Tusi, Sh., Chamani, J.: Multi-spectroscopic investigations of aspirin and colchicine interactions with human hemoglobin: binary and ternary systems. J. Solution Chem. 40, 1905–1931 (2011)

    Article  CAS  Google Scholar 

  59. Cui, F.L., Fan, J., Li, W., Fan, Y.C., Hu, Z.D.: Fluorescence spectroscopy studies on 5-aminosalicylic acid and zinc 5-aminosalylicylate interaction with human serum albumin. J. Pharm. Biomed. Anal. 34, 189–197 (2004)

    Article  CAS  Google Scholar 

  60. Liu, X.F., Xia, Y.M., Fang, Y.: Effect of metal ions on the interaction between bovine serum albumin and berberine chloride extracted from a traditional Chinese herb Coptis chinensis franch. J. Inorg. Biochem. 99, 1449–1457 (2005)

    Article  CAS  Google Scholar 

  61. Garai, K., Sengupta, P., Sahoo, B., Maidi, S.: Selective destabilization of soluble amyloid beta oligomas by divalent metal ions. Biochem. Biophys. Res. Commun. 345, 210–215 (2006)

    Article  CAS  Google Scholar 

  62. Sissi, C., Marangon, E., Chemello, A., Noble, C.G., Maxwell, A., Palumbo, M.: The effect of metal ions on the structure and stability of the DNA Gyrase B protein. J. Mol. Biol. 353, 1152–1160 (2005)

    Article  CAS  Google Scholar 

  63. Matei, I., Hillebrand, M.: Interaction of kaempferol with human serum albumin: A fluorescence and circular dichroism study. J. Pharm. Biomed. Anal. 51, 768–773 (2010)

    Article  CAS  Google Scholar 

  64. Kelly, S.M., Jess, T.J., Price, N.C.: How to study proteins by circular dichroism. Biochim. Biophys. Acta 1751, 119–139 (2005)

    Article  CAS  Google Scholar 

  65. Whitford, D.: The Proteins Structure and Function, pp. 83–97. John Wiley and Sons, West Sussex (2005)

    Google Scholar 

  66. Raghuraman, H., Chattopadhyay, A.: Organization and dynamics of melittin in environments of graded hydration: A fluorescence approach. Langmuir 19, 10332–10341 (2003)

    Article  CAS  Google Scholar 

  67. Chattopadhyay, A.: Exploring membrane organization and dynamics by the wavelength-selective fluorescence approach. Chem. Phys. Lipids 122, 3–17 (2003)

    Article  CAS  Google Scholar 

  68. Shang, L., Wang, Y.Z., Jiang, J.G., Dong, S.J.: pH-dependent protein conformational changes in albumin: gold nanoparticle bioconjugates: A spectroscopic study. Langmuir 23, 2714–2721 (2007)

    Article  CAS  Google Scholar 

  69. Demchenko, A.P.: The red-edge effects: 30 years of exploration. J. Lumin. 17, 19–42 (2002)

    Article  CAS  Google Scholar 

  70. Klajnert, B., Stanislawska, L., Bryszewska, M., Palecz, B.: Interactions between PAMAM dendrimers and bovine serum albumin. Biochim. Biophys. Acta 1648, 115–126 (2003)

    Article  CAS  Google Scholar 

  71. Zhang, H.M., Wang, Y.Q., Jiang, M.L.: A fluorimetric study of the interaction of C.I. Solvent Red 24 with haemoglobin. Dyes Pigments. 82, 156–163 (2009)

    Article  CAS  Google Scholar 

  72. Rodríguez-Cuesta, M.J., Boque, R., Rius, F.X., Zamora, D.P., Galera, M.M., Frenich, A.G.: Development and validation of a method for determining pesticides in groundwater from complex overlapped HPLC signals and multivariate curve resolution. Anal. Chim. Acta 491, 47–56 (2003)

    Article  Google Scholar 

  73. Trevisan, M.G., Poppi, R.J.: Determination of doxorubicin in human plasma by excitation-emission matrix fluorescence and multi-way analysis. Anal. Chim. Acta 493, 69–81 (2003)

    Article  CAS  Google Scholar 

  74. Lakowicz, J.R.: Principles of Fluorescence Spectroscopy. Springer Science and Business Media, New York, pp. 52, 277 and 530 (2006)

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Acknowledgments

The financial support of the Research Council of the Mashhad Branch, Islamic Azad University, is gratefully acknowledged. The authors also thank Dr. Ljungberg for the English editing.

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Authors and Affiliations

  1. Department of Biology, Faculty of Sciences, Mashhad Branch, Islamic Azad University, Mashhad, Iran

    Behnaz Bakaeean, Mona Kabiri, Hedieh Iranfar & Jamshidkhan Chamani

  2. Medical Chemistry Department, School of Pharmacy, Mashhad University of Medical Sciences, Mashhad, Iran

    Mohammad Reza Saberi

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  1. Behnaz Bakaeean
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  2. Mona Kabiri
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Correspondence to Mona Kabiri or Jamshidkhan Chamani.

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Bakaeean, B., Kabiri, M., Iranfar, H. et al. Binding Effect of Common Ions to Human Serum Albumin in the Presence of Norfloxacin: Investigation with Spectroscopic and Zeta Potential Approaches. J Solution Chem 41, 1777–1801 (2012). https://doi.org/10.1007/s10953-012-9895-3

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