Skip to main content
SpringerLink
Log in

Interaction of bovine serum albumin with nonionic surfactant Tween 80 in aqueous solutions: Complexation and association

  • Published:
Colloid Journal Aims and scope Submit manuscript

Abstract

It is shown by the methods of precision tensiometry, quasi-elastic light scattering, and UV, IR, and fluorescent spectroscopies that the properties of binary aqueous solutions with a constant concentration of bovine serum albumin and different concentrations of the nonionic surfactant Tween 80 (1 × 10–7−6 × 10−2 M) are determined mainly by the complexation and formation of a new phase. The complexation occurs owing to specific interactions (hydrogen bonding) between polar groups of Tween 80 and protein molecules. The solubility in water and surface activity of a 1: 1 Tween 80-protein complex are determined. At the concentrations above the break point on surface tension isotherms (conditionally corresponding to critical association concentration), the particles are formed with radii varying from 16 to 350 nm. At a molar nonionic surfactant/protein ratio in the range of 6–10, the additional binding of Tween 80 molecules by the particles of the new phase due to hydrophobic interactions is observed.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

References

  1. Holmberg, K., Jonson, B., Kronberg, B., and Lindman, B., in Surfactants and Polymers in Aqueous Solution, New York, 2004, p. 250.

  2. Lissi, E., Abun, E., Lanio, M., and Alvares, C., Biochem. Biophys. Methods, 2002, vol. 50, p. 261.

    CAS  Google Scholar 

  3. Knox, W.L. and Parshall, T.O., J. Colloid Interface Sci., 1970, vol. 33, p. 16.

    Article  CAS  Google Scholar 

  4. Ananthapadmanabhan, P.K., Protein-Surfactant Solutions, Boca Raton: CRC, 1993, p. 320.

    Google Scholar 

  5. Reinolds, J.A., Biochemistry, 1970, vol. 9, p. 1232.

    Google Scholar 

  6. Cabane, B. and Duplessix, R., J. Phys. (Paris), 1982, vol. 43, p. 1529.

    CAS  Google Scholar 

  7. Caetano, W., Ferreira, M., and Oliveira, O., Colloids Surf., B, 2004, vol. 38, p. 21.

    Article  CAS  Google Scholar 

  8. Choi, J.-K., Ho, J., Curry, S., et al., J. Lipid Res., 2002, vol. 43, p. 1000.

    CAS  Google Scholar 

  9. Brown, J.R. and Shockley, P., in Lipid-Protein Interaction, New York: Wiley, 1982, vol. 1, p. 60.

    Google Scholar 

  10. Carter, D. and Ho, J.X., in Advances in Protein Chemistry, New York: Academic, 1994, vol. 45, p. 153.

    Google Scholar 

  11. Peters, T., in Advances in Protein Chemistry, New York: Academic, 1985, vol. 37, p. 161.

    Google Scholar 

  12. Moore, P.N., Puvvada, S., and Blankschtein, D., Langmuir, 2003, vol. 19, p. 1009.

    Article  CAS  Google Scholar 

  13. Lu, R.-C., Cao, A.-N., Lai, L.-H., et al., Colloids Surf., B, 2005, vol. 41, p. 139.

    CAS  Google Scholar 

  14. Durchschlag, H., Tiefenbach, K.-J., Gebauer, S., and Jaenicke, R., J. Mol. Struct., 2001, vols. 563–564, p. 449.

    Google Scholar 

  15. Nielsen, A.D., Borch, K., and Westh, P., Biochim. Biophys. Acta, 2000, vol. 1479, p. 321.

    CAS  Google Scholar 

  16. Deep, S. and Ahluwalia, J.C., Phys. Chem. Chem. Phys., 2001, vol. 3, p. 4583.

    Article  CAS  Google Scholar 

  17. Shweizer, B., Zanette, D., and Itri, R., J. Colloid Interface Sci., 2004, vol. 277, p. 285.

    Google Scholar 

  18. Santos, S.F., Zanette, D., Fisher, H., and Itri, R., J. Colloid Interface Sci., 2003, vol. 262, p. 400.

    Article  CAS  Google Scholar 

  19. Moriyama, Y., Kawasaka, Y., and Takeda, K., J. Colloid Interface Sci., 2003, vol. 257, p. 41.

    Article  CAS  Google Scholar 

  20. Gelamo, E.L., Itri, R., Alonso, A., et al., J. Colloid Interface Sci., 2004, vol. 277, p. 471.

    Article  CAS  Google Scholar 

  21. Sen, M., Mitra, S.P., and Chattoraj, D.K., Colloids Surf., 1981, vol. 2, p. 287.

    Article  Google Scholar 

  22. Rafati, A.A., Gharibi, H., and Iloukhani, H., Phys. Chem. Liquids, 2003, vol. 41, p. 509.

    CAS  Google Scholar 

  23. Wahlgren, M., Kedstrom, J., and Arnebrant, T., J. Dispersion Sci. Technol., 1997, vol. 18, p. 449.

    CAS  Google Scholar 

  24. Arakawa, T. and Kita, Y., J. Pharm. Sci., 2000, vol. 82, p. 646.

    Google Scholar 

  25. Yampol’skaya, G.P., Zadymova, N.M., Tarasevich, B.N., and Elenskii, A.A., Vestn. Mosk. Univ., Ser. 2: Khim., 2004, vol. 45, p. 371.

    CAS  Google Scholar 

  26. Pugachevich, P.P., Zh. Fiz. Khim., 1962, vol. 36, p. 1107.

    CAS  Google Scholar 

  27. Kunts, I.D. and Kauzmann, W., Adv. Protein Chem., 1974, vol. 28, p. 239.

    Google Scholar 

  28. Carrasquillo, K.G., Cordero, R.A., Ho, S., et al., Pharm. Pharmacol. Commun., 1998, vol. 4, p. 563.

    CAS  Google Scholar 

  29. Koppel, D.E., J. Chem. Phys., 1972, vol. 57, p. 4814.

    Article  CAS  Google Scholar 

  30. Stanley, M.E., Introduction to Phase Transitions and Critical Phenomena, London: Oxford Univ. Press, 1971, p. 40.

    Google Scholar 

  31. Hiemenz, P., Principles of Colloid and Surface Chemistry, New York: Marcel Dekker, 1986, p. 86.

    Google Scholar 

  32. Ogino, K., Able, M., and Deccer, M., Surfactant Sci. Ser., 1983, no. 46, p. 10.

  33. Cooke, D.J., Dong, C.C., and Thomas, R.K., Langmuir, 2000, vol. 16, p. 6546.

    Article  CAS  Google Scholar 

  34. Vyustnek, R., Tsastrov, L., and Krechmar, G., Kolloidn. Zh., 1985, vol. 57, p. 462.

    Google Scholar 

  35. Shchukin, E.D., Pertsov, A.V., and Amelina, E.A., Kolloidnaya khimiya (Colloid Chemistry), Moscow: Vysshaya Shkola, 2004.

    Google Scholar 

  36. Almeda, N.L., Oliveria, C.L.P., Torriani, I.L., and Loh, W., Colloids Surf., B, 2004, vol. 38, p. 67.

    Google Scholar 

  37. Freifelder, D., Applications to Biochemistry and Molecular Biology, San Francisco: Freeman, 1976.

    Google Scholar 

  38. Barltrop, L. and Coyle, J., Excited States in Organic Chemistry, London: Wiley, 1975.

    Google Scholar 

  39. Moller, M. and Denicova, A., Biochem. Mol. Biol. Educ., 2002, vol. 30, p. 175.

    CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Department of Chemistry, Moscow State University, Vorob’evy gory, 119992, Russia

    N. M. Zadymova, G. P. Yampol’skaya & L. Yu. Filatova

Authors
  1. N. M. Zadymova
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. G. P. Yampol’skaya
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. L. Yu. Filatova
    View author publications

    You can also search for this author in PubMed Google Scholar

Additional information

Original Russian Text © N.M. Zadymova, G.P. Yampol’skaya, L.Yu. Filatova, 2006, published in Kolloidnyi Zhurnal, 2006, Vol. 68, No. 2, pp. 187–197.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Zadymova, N.M., Yampol’skaya, G.P. & Filatova, L.Y. Interaction of bovine serum albumin with nonionic surfactant Tween 80 in aqueous solutions: Complexation and association. Colloid J 68, 162–172 (2006). https://doi.org/10.1134/S1061933X06020074

Download citation

  • Received:

  • Issue Date:

  • DOI: https://doi.org/10.1134/S1061933X06020074

Keywords

Search

Navigation