Isothermal titration calorimetry (ITC) is a thermodynamic technique that allows the study of the interactions of two species. When these two species interact, heat is either generated or absorbed. By measuring these interaction heats, binding constants (K), reaction stoichiometry (n), and thermodynamic parameters including enthalpy (H) and entropy (S) can be accurately determined. In addition, varying the temperature of the experiment allows the determination of the heat capacity (Cp) for the reaction.
The CSC ITC allows researchers to study almost any kind of interaction, including solutes with immobilized enzymes, tissue samples, or other solid materials in suspension. Titration experiments are typically fast (approximately 1 hour) yielding accurate values of K (in the range of 102 to 108 M-1), n, H, and S. In addition, analytical data (ex. enzyme assay) or kinetic data (for slow reactions) may be obtained in a batch injection experiment.
The CSC ITC may also be used to study the decomposition/stability of organic (ex. drugs) and inorganic materials over time (days to weeks). This is particularly useful for determining shelf/storage life of drugs, etc.
Applications
Protein interactions with other proteins, lipids, carbohydrates, DNA, ligands, nucleic acids, etc.
Enzyme interactions with co-enzymes, inhibitors, substrates, drugs, etc.
Biopolymer interactions with other biopolymers, drugs, ligands, etc.
Enzyme activity analysis
Antibody studies
Cell metabolism
Drug receptor interactions
Polymerizations, surfactants, metal chelation, etc.
H) and entropy (
