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Updated: Jul 15, 2026

Differential Scanning Calorimetry — A Method for Assessing the Thermal Stability and Conformation of Protein Antigen
08:13

Differential Scanning Calorimetry — A Method for Assessing the Thermal Stability and Conformation of Protein Antigen

Published on: March 4, 2017

Enthalpy-entropy compensation in the transition of a monospecific antibody towards antigen-binding promiscuity

Jonghoon Kang, Andrew S Warren

    Molecular Immunology
    |April 28, 2007
    PubMed

    In a recent article published in Molecular Immunology (Dimitrov, J.D., Lacroix-Desmazes, S., Kaveri, S.V., Vassilev, T.L., 2007. Transition towards antigen-binding promiscuity of a monospecific antibody. Mol. Immunol. 44, 1854-1863.), the authors perform kinetic and thermodynamic analyses using a surface plasmon resonance-based technique to explain polyspecificity of antibodies in terms of molecular mechanisms. They found that after the antibody was exposed to urea, a protein destabilizing agent, it had the same affinity as the native state and that the two forms of the antibody use two distinct thermodynamic pathways for binding to the same antigen. In this letter, we report our analysis of these results in terms of equilibrium thermodynamics to show that the specificity transition of the antibody exhibits enthalpy-entropy compensation.

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