Ligand binding to multiple equivalent sites with steric hindrance

Matthew R. Pincus, Charles DeLisi, Marc Rendell

Research output: Contribution to journalArticlepeer-review

5 Scopus citations


A general model is developed for the binding of ligands to multiple receptor sites in which steric blockage of sites is taken into account. Analytical expressions for extent of ligand binding as a function of ligand concentration are derived employing a stochastic matrix approach. Using simple numerical techniques to evaluate these expressions it is possible to obtain the inherent affinity of each site for a ligand, the number of sites available and the number of sites excluded when a ligand binds to any site. The expressions derived here are contrasted with other expressions based on simple equilibrium considerations in which there are no interactions between sites and no interactions between ligands in different sites. It is shown that the expressions derived here predict significant departures from linearity in Scatchard plots and a strong negative cooperatively, especially toward the saturation limit.

Original languageEnglish
Pages (from-to)392-396
Number of pages5
JournalBiochimica et Biophysica Acta - General Subjects
Issue number3-4
StatePublished - 17 Jul 1981
Externally publishedYes


  • Ligand binding
  • Receptor site
  • Steric hindrance


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