At iNANO, the groups of Daniel Otzen and Jørgen Kjems have access to a broad array of techniques to study protein-protein interactions in vitro and in vivo. In addition to conventional approaches (isothermal titration calorimetry, biolayer interferometry, surface plasmon resonance, fluorescence and circular dichroism with stopped-flow kinetics and NMR), we have recently acquired a FIDA (Flow-Induced Dispersion Analysis) instrument which allows us to measure the hydrodynamic radii of proteins and protein complexes by microfluidics and thus measure binding affinities. This can be carried out in complex media like plasma and is adaptable to high-throughput screening. Resulting hits can be validated in cellula using flow cytometry approaches.

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