The confirmation of drug interactions with target proteins is a critical step in every hit validation program. The use of label-free biophysical techniques such as SPR and Isothermal Titration Calorimetry (ITC) yields valuable insights into affinity, stoichiometry and mechanism of binding that are unavailable by other methods. By combining the power of these two techniques, you can obtain a complete picture of the binding interaction:
• Determine gold standard KD values • Measure binding kinetics • Determine binding mechanisms and stoichiometry • Assess binding in label-free environment
Abstract: Confirmation of small molecule interactions with target proteins is a key step in drug discovery programs. The use of label free biophysical techniques will yield important information on the binding interaction giving confidence that medicinal chemistry efforts are focused on the appropriate compounds. This presentation will describe the use of Biacore™ systems - and MicroCal™ isothermal titration calorimetry (ITC) systems as complementary biophysical techniques for providing reliable hit validation. The combination of these technologies can provide a more complete picture of the biomolecular interaction. This includes information on the rate of complex formation, complex stability, as well as thermodynamic insights into the binding mechanism.
A software package will also be discussed that uses affinity data from Biacore experiments to optimize MicroCal Auto-iTC200 experimental design. Kinetic and thermodynamic data are then collected in and Excel™ spreadsheet for facilitated comparison. This brings together two important additional parameters for rational discovery of more selective and drug like compounds: target residence time and enthalpic efficiency.
Presenter: Brian Lightbody GE Healthcare Biography >>
Presenter: Dr Ronan O'Brien GE Healthcare Biography >>
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