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Determination of High-affinity Antibody-antigen Binding Kinetics Using Four Biosensor Platforms
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Use of biosensors to measure the kinetics of antibody-antigen interactions

A J George1

  • 1Department of Immunology, Imperial College School of Medicine, London, UK.

Methods in Molecular Medicine
|February 22, 2011
PubMed

The affinity and kinetics of antibody-antigen interactions are increasingly realized to be important parameters in determining the usefulness of antibodies in both in vivo and in vitro settings (1). As discussed in Chapter 1, the affinity of an antibody (given by the association or dissociation equilibrium constants; Ka and K(d)) gives information about how much antibody will be bound to the antigen at equilibrium, or how much antibody will be required for a particular proportion of the antigen to be bound. The kinetics of the interaction (given by the association and dissociation rate constants; k (ass) and kdiss) tell how rapidly the antibody-antigen complex is formed and, once formed, how rapidly it dissociates.

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