Dynamic interactions involving biomolecules drive and regulate all biological processes, making interaction analysis a key area of academic and industrial research and development. A variety of biophysical techniques are used in this field, including Nuclear Magnetic Resonance (NMR), Isothermal Titration Calorimetry (ITC), biosensors (such as SPR and BLI) and fluorescence-based assays. 

Over the years, clear trends in interaction analysis have driven towards increased ease of use of the advanced techniques, despite the increasing complexity of biomolecules and binding modes being studied.
While methodologies and technologies in interaction analysis continue to evolve, one fundamental prerequisite to the success remains constant: good control over the quality of interacting species, their complexes, and conditions for the binding process. Overlooking this requirement could result in poor performance of a biophysical technique, misleading and irreproducible results and lack of convergence with orthogonal and complementary data generated in a project.

This presentation will give examples which highlight the need for ensuring sample quality and observing good experimental practices for the generation of meaningful and reliable binding data. Case study examples will be given to illustrate the impact of early in-solution profiling of the stability and homogeneity of biomolecules and ligands with: 

•    Dynamic Light Scattering (DLS)
•    Differential Scanning Calorimetry (DSC)
•    Multi-Detection Size Exclusion Chromatography (SEC) and
•    Taylor Dispersion Analysis (TDA)
on the success of research projects in Drug Discovery.