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SANS/SAXS study of the BSA solvation properties in aqueous urea solutions via a global fit approach

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Abstract

We report on the solvation properties and intermolecular interactions of a model protein (bovine serum albumine, BSA) in urea aqueous solutions, as obtained by combining small-angle neutron and X-ray scattering experiments. According to a global fit strategy, all the whole set of scattering curves are analysed by considering a unique model which includes the BSA structure, the protein-protein interactions and the thermodynamic exchange process of water/urea molecules at the protein solvent interface. As a main result, the equilibrium constant that accounts for the difference in composition between the bulk solvent and the protein solvation layer is derived. Results confirm that urea preferentially sticks to the protein surface, inducing a noticeable change in both the repulsive and the attractive interaction potentials.

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Acknowledgments

We thank Fondazione Cariverona for financial support.

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Authors and Affiliations

  1. Dipartimento di Scienze applicate ai Sistemi Complessi, Università Politecnica delle Marche, Via Brecce Bianche, 60019, Ancona, Italy

    Raffaele Sinibaldi, Maria Grazia Ortore, Francesco Spinozzi & Paolo Mariani

  2. HASYLAB at the German Electron Synchrotron DESY, Hamburg, Germany

    Sérgio de Souza Funari

  3. Laboratoire Leon Brillouin (CEA/CNRS), Saclay, 91191, Gif-sur-Yvette, France

    José Teixeira

Authors
  1. Raffaele Sinibaldi
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  2. Maria Grazia Ortore
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  3. Francesco Spinozzi
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  4. Sérgio de Souza Funari
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  5. José Teixeira
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  6. Paolo Mariani
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Corresponding author

Correspondence to Raffaele Sinibaldi.

Additional information

Advanced neutron scattering and complementary techniques to study biological systems. Contributions from the meetings, “Neutrons in Biology”, STFC Rutherford Appleton Laboratory, Didcot, UK, 11–13 July and “Proteins At Work 2007”, Perugia, Italy, 28–30 May 2007.

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Sinibaldi, R., Ortore, M.G., Spinozzi, F. et al. SANS/SAXS study of the BSA solvation properties in aqueous urea solutions via a global fit approach. Eur Biophys J 37, 673–681 (2008). https://doi.org/10.1007/s00249-008-0306-z

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  • DOI: https://doi.org/10.1007/s00249-008-0306-z

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