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Affinity determination of biomolecules: a kinetic model for the analysis of pre-equilibrium titration curves

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Abstract

Equilibrium titration curves have been used to determine the affinity of biomolecules using a variety of platforms and technologies. Such measurements, however, are experimentally limited by the time that is needed for the system to reach the equilibrium, which may exceed the time during which the studied biomolecules are stable. We propose here a kinetic model to analyze titration curves obtained prior to full equilibration of the system.

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Author notes

  1. Marc Vanhove

    Present address: ThromboGenics N.V., Gaston Geenslaan 1, 3001, Leuven, Belgium

Authors and Affiliations

  1. Faculté des Sciences Appliquées, Institut de Mathématique (B37), Quartier Polytech 1, Allée de la Découverte 12, Sart Tilman, 4000, Liège, Belgium

    Emilie Vanhove

  2. Marc Vanhove Consultancy, 4100, Boncelles, Belgium

    Marc Vanhove

Authors
  1. Emilie Vanhove
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  2. Marc Vanhove
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Correspondence to Marc Vanhove.

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Vanhove, E., Vanhove, M. Affinity determination of biomolecules: a kinetic model for the analysis of pre-equilibrium titration curves. Eur Biophys J 47, 961–966 (2018). https://doi.org/10.1007/s00249-018-1318-y

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  • DOI: https://doi.org/10.1007/s00249-018-1318-y

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