Allosteric binding cooperativity in a kinetic context

Óscar Díaz, Victor Martín, Pedro Renault, David Romero, Jesús Giraldo*, Antoni Guillamon

*Corresponding author for this work

Research output: Contribution to journalArticleResearchpeer-review


Allosteric modulators are of prime interest in drug discovery. These drugs regulate the binding and function of endogenous ligands, with some advantages over orthosteric ligands. A typical pharmacological parameter in allosteric modulation is binding cooperativity. This property can yield unexpected but illuminating results when decomposed into its kinetic parameters. Using two reference models (the allosteric ternary complex receptor model and a heterodimer receptor model), a relationship has been derived for the cooperativity rate constant parameters. This relationship allows many combinations of the cooperativity kinetic parameters for a single binding cooperativity value obtained under equilibrium conditions. This assessment may help understand striking experimental results involving allosteric modulation and suggest further investigations in the field.

Original languageEnglish
Article number103441
JournalDrug Discovery Today
Issue number2
Publication statusPublished - Feb 2023


  • allosteric modulation
  • binding cooperativity
  • binding kinetics
  • cooperativity rate constant
  • GPCRs
  • heterodimer receptor
  • rate constant
  • residence time


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