Isothermal Titration Calorimetry

Isothermal titration calorimetry (ITC) characterizes the thermodynamic driving forces of critical molecular interactions and defines molecular stabilities, being an essential tool in the design of effective biomedical and pharmaceutical treatments. This analysis is based on the accurate measurement of the rate of heat absorbed or evolved when the biomolecule of interest interacts specifically or non-specifically with another macromolecule or ligand.

Application examples:

• Protein folding and misfolding
• Binding interactions: protein-protein, protein-DNA/RNA, protein-small ligands, DNA/RNA-small molecules
• Drug discovery and development:
• Determination of binding affinity
• Candidate selection and optimization
• Measurement of thermodynamics and active concentration
• Characterization of mechanism of action
• Confirmation of intended binding targets in small molecule drug discovery
• Determination of binding specificity and stoichiometry
• Validation of IC50 and EC50 values during hit-to-lead
• Measurement of enzyme kinetics
  

The available equipment at Biolab is the TA™ Nano ITC, designed to improve laboratory productivity and efficiency by performing high-sensitivity analyses on nanomolar quantities of biomolecule. The NanoAnalyze™ software provides a quick and easy data analysis.

Publications with the TA™ Nano ITC:

• Song, Y. et al. A Novel Manno-Oligosaccharide Binding Protein Identified in Alkaliphilic Bacillus sp. N16-5 Is Involved in Mannan Utilization. PLoS One 11, e0150059 (2016).
• Whitfield, J. H. et al. Construction of a robust and sensitive arginine biosensor through ancestral protein reconstruction. Protein Sci. 24, 1412–22 (2015).
• Schelhorn, C. et al. RNA recognition and self-association of CPEB4 is mediated by its tandem RRM domains. Nucleic Acids Res. 42, 10185–95 (2014).