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Thermodynamic study of indoxylsulfate interaction with human serum albumin and competitive binding with p-cresylsulfate

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Abstract

Indoxylsulfate (IS) and p-cresylsulfate (PCS) are natural compounds endowed with toxicity. These molecules are harmful to the environment and removed by the procedure of dialysis. Knowledge of their interaction with biologic compounds such as proteins and particularly human serum albumin (HSA) is limited. This study was therefore designed to determine the thermodynamic parameters of the interaction of IS with HSA and in competition with PCS. Results showed that IS binding is moderate (K a = 1,750 ± 39 M−1). The interaction is mainly electrostatic (∆H° = −36.2 ± 1.7 kJ mol−1) and yields a modification of conformation upon binding (∆conf S° < 0). The thermodynamic parameters obtained at different temperatures show an enthalpy–entropy compensation process. Competition with PCS reveals that affinity for IS decreased by 36 %, with profound modification of the binding forces involved and a release of PCS from the binding site.

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Acknowledgments

Authors would like to thank Raymond Calaf, Philippe Charpiot and Caroline Montet for their helpful discussions.

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Authors and Affiliations

  1. Unité Chimie Physique, Prévention des Risques et Nuisances Technologiques, Faculté de Pharmacie, Aix-Marseille Université, UMR CNRS 7263 IMBE, 13005, Marseille, France

    David Bergé-Lefranc, Florence Chaspoul & Philippe Gallice

  2. Laboratoire d’Hématologie Immunologie, Faculté de Pharmacie, Aix-Marseille Université INSERM U608, 13005, Marseille, France

    Claire Cérini & Philippe Brunet

Authors
  1. David Bergé-Lefranc
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  2. Florence Chaspoul
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  3. Claire Cérini
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  4. Philippe Brunet
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  5. Philippe Gallice
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Correspondence to Philippe Gallice.

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Bergé-Lefranc, D., Chaspoul, F., Cérini, C. et al. Thermodynamic study of indoxylsulfate interaction with human serum albumin and competitive binding with p-cresylsulfate. J Therm Anal Calorim 115, 2021–2026 (2014). https://doi.org/10.1007/s10973-013-3067-6

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  • DOI: https://doi.org/10.1007/s10973-013-3067-6

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