Mathematical model for determining the binding constants between immunoglobulins, bivalent ligands, and monovalent ligands

Eric T. MacK, Linda Cummings, Raquel Perez-Castillejos

Research output: Contribution to journalArticlepeer-review

8 Scopus citations

Abstract

This paper analyzes the equilibria between immunoglobulins (R2), homo-bifunctional ligands (L2), monovalent ligands (I), and their complexes. We present a mathematical model that can be used to estimate the concentration of each species present in a mixture of R 2, L 2, and I, given the initial conditions defining the total concentration of R2, L2, I, and four dissociation constants (Kdinter, Kdintra, K dmono, and α). This model is based on fewer assumptions than previous models and can be used to describe exactly a broad range of experimental conditions. A series of curves illustrates the dependence of the equilibria upon the total concentrations of receptors and ligands, and the dissociation constants. We provide a set of guidelines for the design and analysis of experiments with a focus on estimating the binding constants from experimental binding isotherms. Two analytical equations relate the conditions for maximum aggregation in this system to the binding constants. This model is a tool to quantify the binding of immunoglobulins to antigens and a guide to understanding and predicting the experimental data of assays and techniques that employ immunoglobulins.

Original languageEnglish (US)
Pages (from-to)1641-1652
Number of pages12
JournalAnalytical and Bioanalytical Chemistry
Volume399
Issue number4
DOIs
StatePublished - Feb 2011

All Science Journal Classification (ASJC) codes

  • Analytical Chemistry
  • Biochemistry

Keywords

  • Affinity
  • Aggregation
  • Antibody
  • Binding isotherm
  • Bivalent ligand

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