Understanding Binding Interaction Workflow Solutions: Save Time and Material
In drug discovery, selection of compound hits with a potential for further development requires a full characterization of binding kinetics. Biophysical techniques such as isothermal titration calorimetry (ITC) and Grating-Coupled Interferometry (GCI) provide information on the global binding mechanisms of protein-protein or protein-ligand interaction, essential for hit characterization.
In this webinar, May Poh Lay, Senior Applications Specialist at Creoptix, will explain why the measurement of kinetics is critical when screening molecules, outlining the GCI technology behind WAVEsystem, how you can use the system, and the associated benefits. The Creoptix™ WAVEsystem puts a breakthrough level of kinetics analysis at your fingertips by pushing the boundaries of affinity range and sample compatibility.
We know how tightly a compound binds to its target, but what are the driving forces? The answer lies with Isothermal Titration Calorimetry (ITC). Significant research done with ITC shows binding interactions driven by enthalpic contributions are more specific, leading to less off-target binding resulting in fewer side effects.1 There are three main methodologies to consider when using ITC:
- Enthalpy screen—understanding the thermodynamic driving forces when KD is known or screening compounds (ΔH and TΔS).
- Incremental titration—Well established traditional ITC experiment providing a full thermodynamic binding characterization (KD, n, and ΔH)
- Continuous titration— Full binding characterization with shorter experimental run time than traditional ITC experiments
1. Ohtaka, et al. Protein Sci. 11, 1908-1916 (2002)