Isothermal Titration Calorimetry
For characterization of molecular interactions, including determination of affinity constants, a titration setup is typically used. The heat generated after each injection is used as a relative measure to quantify the number of reactions taking place. As the system comes closer to saturation, fewer interactions occur and the signals therefore are lowered. By applying the law of mass action, affinity constants can be derived from such data. ITC is particularly powerful when investigating low affinity interactions. These features enable ITC for:
- Biomolecular interaction studies with low affinity binding (e.g. viral attachment to cellular structures [1])
- Sorption characteristics of polymeric materials (e.g. PDMS, with and without recognition structures embedded [4], MIPs)
Besides determination of affinity constants, enzymatic reactions or the metabolic rate of living microorganisms can be studied. The heat is detected in a time-resolved manner, so even the kinetics of slow interactions can be studied.