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Fluorescence Study on the Interaction of Bovine Serum Albumin with P-Aminoazobenzene

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Abstract

In this paper, the interaction between p-aminoazobenzene (PAAB) and BSA was investigated mainly by fluorescence quenching spectra, circular dichroism (CD) and three-dimensional fluorescence spectra under simulative physiological conditions. It was proved that the fluorescence quenching of BSA by PAAB was mainly a result of the formation of a PAAB-BSA complex. The modified Stern-Volmer quenching constant K a and the corresponding thermodynamic parameters ΔH, ΔG and ΔS at different temperatures were calculated. The results indicated that van der Waals interactions and hydrogen bonds were the predominant intermolecular forces in stabilizing the complex. The distance r = 4.33 nm between the donor (BSA) and acceptor (PAAB) was obtained according to Förster’s non-radioactive energy transfer theory. The synchronous fluorescence, CD and three-dimensional fluorescence spectral results showed that the hydrophobicity of amino acid residues increased and the losing of α-helix content (from 63.57 to 51.83%) in the presence of PAAB. These revealed that the microenvironment and conformation of BSA were changed in the binding reaction.

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References

  1. Carter DC, Ho JX (1994) The structure of serum albumin. Adv Prot Chem 45:153–203

    Article  CAS  Google Scholar 

  2. Zsila F, Bikadi Z, Simonyi M (2003) Probing the binding of the flavonoid quercetin to human serum albumin by circular dichroism, electronic absorption spectroscopy and molecular modelling methods. Biochem Pharmacol 65:447–456

    Article  PubMed  CAS  Google Scholar 

  3. Chatterjee S, Srivastava TS (2000) Spectral investigations of the interaction of some porphyrins with bovine serum albumin. J Porphyr Phthalocya 4:147–157

    Article  CAS  Google Scholar 

  4. Hu YJ, Liu Y, Wang JB et al (2004) Study of the interaction between monoammonium glycyrrhizinate and bovine serum albumin. J Pharm Biomed Anal 36:915–919

    Article  PubMed  CAS  Google Scholar 

  5. Hu YJ, Liu Y, Shen XS et al (2005) Studies on the interaction between 1-hexylcarbamoyl-5-fluorouracil and bovine serum albumin. J Mol Struct 738:143–147

    Article  CAS  Google Scholar 

  6. Wang YQ, Zhang HM, Zhang GC et al (2007) Spectroscopic studies on the interaction between silicotungstic acid and bovine serum albumin. J Pharm Biomed Anal 43:1869–1875

    Article  PubMed  CAS  Google Scholar 

  7. Guharay J, Sengupta B, Sengupta PK (2001) Protein-flavonol interaction: fluorescence spectroscopic study. Proteins 43:75–81

    Article  PubMed  CAS  Google Scholar 

  8. Zolese G, Falcioni G, Bertoli E et al (2000) Steady-state and time resolved fluorescence of albumins interacting with N-oleylethanolamine, a component of the endogenous N-acylethanolamines. Proteins 40:39–48

    Article  PubMed  CAS  Google Scholar 

  9. Gelamo EL, Tabak M (2000) Spectroscopic studies on the interaction of bovine (BSA) and human (HSA) serum albumins with ionic surfactants. Spectrochim Acta Pt A-Mol Bio 56:2255–2271

    Article  Google Scholar 

  10. Zollinger H (1991) Color chemistry: synthesis, properties, and applications of organic. Dye. Pigment. 2nd edn. VCH, Weinheim

    Google Scholar 

  11. Dirksen A, Zuidema E, Williams RM, De Cola L (2002) Photoactivity and pH sensitivity of methyl orange functionalized poly (Propyleneamine) dendrimers. Macromolecules 35:2743–2747

    Article  CAS  Google Scholar 

  12. Wang XG, Kumar J, Tripathy SK et al (1997) Epoxy-based nonlinear optical polymers from post azo coupling reaction. Macromolecules 30:219–225

    Article  CAS  Google Scholar 

  13. Ikeda T, Tsutsumi O (1995) Optical switching and image storage by means of azobenzene liquid-crystal films. Science 268:1873–1875

    Article  PubMed  CAS  Google Scholar 

  14. Hugel T, Holland NB, Cattani A et al (2002) Single molecul opto-mechanical cycle. Science 296:1103–1106

    Article  PubMed  Google Scholar 

  15. Kragh-Hansen U (1981) Molecular aspects of ligand binding to serum albumin. Pharmacol Rev 33:17–53

    PubMed  CAS  Google Scholar 

  16. Bhattacharyya M, Chaudhuri U, Poddar RK (1990) Evidence for cooperative binding of CPZ with hemoglobin. Biochem Biophys Res Commun 167:1146–1153

    Article  PubMed  CAS  Google Scholar 

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

    Article  CAS  Google Scholar 

  18. Zhang HX, Huang X, Mei P et al (2006) Studies on the interaction of tricyclazole with â-cyclodextrin and human serum albumin by spectroscopy. J Fluorescence 16:287–294

    Article  CAS  Google Scholar 

  19. Gelamo EL, Silva CHTP, Imasato H, Tabak M (2002) Interaction of bovine and human serum albumins with ionic surfactants: spectroscopy and modeling. Biochim Biophys Acta 1594:84–99

    PubMed  CAS  Google Scholar 

  20. Kang J, Liu Y, Xie MX et al (2004) Interactions of human serum albumin with chlorogenic acid and ferulic acid. Biochim Biophys Acta 1674:205–214

    PubMed  CAS  Google Scholar 

  21. Eftink MR (1991) Fluorescence quenching reactions: probing biological macromolecular structures. In: Dewey TG (ed) Biophysical and biochemical aspects of fluorescence spectroscopy. Plenum, New York

    Google Scholar 

  22. Lakowica JR, Weber G (1973) Quenching of fluorescence by oxygen, a probe for structural fluctuations in macromolecules. Biochemistry 12:4161–4170

    Article  Google Scholar 

  23. Maurice RE, Camillo AG (1981) Fluorescence quenching studies with proteins. Anal Biochem 114:199–212

    Article  Google Scholar 

  24. Ware WR (1962) Oxygen quenching of fluorescence in solution, an experimental study of the diffusion process. J Phys Chem 66:455–458

    Article  CAS  Google Scholar 

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

    Article  PubMed  CAS  Google Scholar 

  26. Lehrer SS (1971) The quenching of the tryptophyl fluorescence of model compounds and of lysozyme by iodide ion. Biochemistry 10:3254–3263

    Article  PubMed  CAS  Google Scholar 

  27. Ross PD, Subramanian S (1981) Thermodynamics of protein association reaction: forces contribution to stability. Biochemistry 20:3096–3102

    Article  PubMed  CAS  Google Scholar 

  28. Liu JQ, Tian JN, Zhang JY et al (2003) Interaction of magnolol with bovine serum albumin: a fluorescence quenching study. Anal Bioanal Chem 376:864–867

    Article  PubMed  CAS  Google Scholar 

  29. Tian JN, Liu JQ, Zhang JY et al (2003) Fluorescence studies on the interactions of barbaloin with bovine serum albumin. Chem Pharm Bull 51:579–582

    Article  PubMed  CAS  Google Scholar 

  30. Jiang M, Xie MX, Zheng D et al (2004) Spectroscopic studies on the interaction of cinnamic acid and its hydroxyl derivatives with human serum albumin. J Mol Struct 692:71–80

    Article  CAS  Google Scholar 

  31. Sklar LA, Hudson BS, Simoni RD (1977) Conjugated polyene fatty acids as fluorescent probes: binding to bovine serum albumin. Biochemistry 16:5100–5108

    Article  PubMed  CAS  Google Scholar 

  32. Cui FL, Fan J, Li JP, Hu ZD (2004) Interactions between 1-benzoyl-4-pchloro-phenyl thiosemicarbazide and serum albumin: investigation by fluorescence spectroscopy. Bioorg Med Chem 12:151–157

    Article  PubMed  CAS  Google Scholar 

  33. Cyril L, Earl JK, Sperry WM (1961) In: Biochemists’ handbook, E & FN Spon, London, pp 84.

  34. Bi S, Song D, Tian Y et al (2005) Molecular spectroscopic study on the interaction of tetracyclines with serum albumins. Spectrochim Acta Pt A-Mol Bio 61:629–636

    Article  CAS  Google Scholar 

  35. Miller JN (1979) Recent advances in molecular luminescence analysis. Proc Anal Div Chem Soc 16:203–208

    CAS  Google Scholar 

  36. Liu JQ, Tian JN, Tian X et al (2004) Interaction of isofraxidin with human serum albumin. Bioorg Med Chem 12:469–474

    Article  PubMed  CAS  Google Scholar 

  37. Yang P, Gao F (2002) The principle of bioinorganic chemistry. Science Press, p 349

  38. Li Y, He W, Liu J et al (2005) Binding of the bioactive component jatrorrhizine to human serum albumin. Biochim Biophys Acta 1722:15–21

    PubMed  CAS  Google Scholar 

  39. Lu ZX, Cui T, Shi QL (1987) In molecular biology, applications of circular dichroism and optical rotatory dispersion, 1st ed. Science Press, pp79–82

  40. Brown KF, Crooks MJ (1976) Displacement of tolbutamide, glibencalmide and chlorpropamide from serum albumin by anionic drugs. Biochem Pharmacol 25:1175–1178

    Article  PubMed  CAS  Google Scholar 

  41. Rosenoer VM, Oratz M, Rothschild MA (eds) (1977) In: Albumin structure, function and uses. Pergamon, New York, pp 113–141

  42. Peters T (1995). In: All about albumin: biochemistry, genetics and medical applications. Academic, San Diego, CA, Chapter 6, pp 251–284

  43. Tian JN, Liu JQ, Hu ZD, Chen XG (2005) Interaction of wogonin with bovine serum albumin. Bioorg Med Chem 13:4124–4129

    Article  PubMed  CAS  Google Scholar 

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Acknowledgements

We gratefully acknowledge the financial support of National Natural Science Foundation of China (Grant no. 30570015, 20621502); Natural Science Foundation of Hubei Province (2005ABC002); Research Foundation of Chinese Ministry of Education ([2006]8-IRT0543); and Chinese 863 program (2007AA06Z407).

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Authors and Affiliations

  1. Department of Chemistry, College of Chemistry and Environmental Engineering, Yangtze University, JingZhou, Hubei, 434025, People’s Republic of China

    Ye-Zhong Zhang, Yan-Xia Liu, Chun-Xia Zhou & Yi Liu

  2. Department of Chemistry, College of Chemistry and Molecular Sciences, Wuhan University, Wuhan, Hubei, 430072, People’s Republic of China

    Ye-Zhong Zhang, Bo Zhou, Xin-Liang Ding & Yi Liu

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  1. Ye-Zhong Zhang
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  2. Bo Zhou
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Correspondence to Yi Liu.

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Zhang, YZ., Zhou, B., Liu, YX. et al. Fluorescence Study on the Interaction of Bovine Serum Albumin with P-Aminoazobenzene. J Fluoresc 18, 109–118 (2008). https://doi.org/10.1007/s10895-007-0247-4

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  • DOI: https://doi.org/10.1007/s10895-007-0247-4

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