Isothermal Titration Calorimetry to Study Plant Peptide Ligand-Receptor Interactions

Judith Lanooij, Elwira Smakowska-Luzan*

*Corresponding author for this work

Research output: Chapter in Book/Report/Conference proceedingChapterAcademicpeer-review

Abstract

The field of plant receptor biology has rapidly expanded in the past three decades. However, the demonstration of direct interaction between receptor-ligand pairs remains a challenge. Identifying and quantifying protein-ligand interactions is crucial for understanding how they regulate certain physiological processes. An important aspect is the quantification of different parameters of the interaction, like binding affinity, kinetics, and ligand specificity that drive the formation of signaling complexes. In this chapter, we discuss Isothermal Titration Calorimetry (ITC) as a label-free technique to measure thermodynamic parameters of ligand binding with high accuracy and reproducibility. We provide a detailed guideline how to design, perform, analyze, and interpret ITC measurements using as an example the interaction between the SCHENGEN3/GASSHO1 (SGN3/GSO1) leucine-rich repeat receptor-like kinase and its sulfated peptide ligand CASPARIAN STRIP INTEGRITY FACTOR 2 (CIF2).

Original languageEnglish
Title of host publicationPlant Peptide Hormones and Growth Factors
EditorsA. Schaller
Place of PublicationNew York
PublisherHumana Press
Pages295-310
Number of pages16
ISBN (Electronic)9781071635117
ISBN (Print)9781071635100
DOIs
Publication statusPublished - 30 Nov 2023

Publication series

NameMethods in Molecular Biology
Volume2731
ISSN (Print)1064-3745
ISSN (Electronic)1940-6029

Keywords

  • Binding affinity
  • Dissociation constant
  • Isothermal Titration Calorimetry (ITC)
  • Peptide binding
  • Protein/peptide interactions
  • Thermodynamic parameters

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