Posted in | Cell Biology

Biomolecules: sample and data quality in interaction analysis - two sides of the same coin

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.


Natalia Markova holds a PhD in Analytical Chemistry from the University of Chemical Technology, Ivanovo, Russia and another PhD in Physical Chemistry from the University of Lund, Sweden. Natalia has extensive experience in the academic and industrial applications of differential and isothermal microcalorimetry, thermal analysis, dynamic light scattering, analytical ultracentrifugation and surface plasmon resonance. Over the last 14 years, she has worked within drug discovery and biopharmaceutical development as a Senior Scientist in the Structural Chemistry department of Biovitrum AB, as Head of Biophysics at the Structural Genomics Consortium, Karolinska Institute, as Associate Director of the biophysical facility in the contract research organization iNovacia AB in Stockholm, Sweden, and as the Senior Customer Relations Manager at GE Healthcare Life Sciences.

In 2014, Natalia joined Malvern Instruments where she continues working on the development and applications of label-free technologies as Principal Scientist – MicroCal and Leader – Scientific Marketing, Biosciences.

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Who should attend?
Researchers active in Drug Discovery, PIs, Project Leaders, Medicinal Chemists, Structural Biologists, Protein Chemists, Core Facility Managers

What will they learn?

  • Factors impacting the quality of ITC and biosensor data in interaction analysis
  • Ways to improve success rates in interaction analysis
  • Is early profiling of in-solution stability and homogeneity of biomolecules and ligands a waste of time?

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