Bestimmung der Affinität über Thermophorese

Molecular Interaction Studies Using Microscale Thermophoresis

Moran Jerabek-Willemsen,1,2 Chistoph J. Wienken,1 Dieter Braun,1 Philipp Baaske,1,2 and Stefan Duhr 1,2

1 Systems Biophysics, Center for Nanoscience, Munich, Germany. 2NanoTemper Technologies GmbH, Munich, Germany

The use of infrared laser sources for creation of localized temperature fields has opened new possibilities for basic research and drug discovery. A recently developed technology, Microscale Thermophoresis (MST), uses this temperature field to perform biomolecular interaction studies. Thermophoresis, the motion of molecules in temperature fields, is very sensitive to changes in size, charge, and solvation shell of a molecule and thus suited for bioanalytics. This review focuses on the theoretical background of MST and gives a detailed overview on various applications to demonstrate the broad applicability 1. Experiments range from the quantification of the affinity of low-molecular-weight binders using fluorescently labeled proteins, to interactions between macromolecules and multi-component complexes like receptor containing liposomes. Information regarding experiment and experimental setup is based on the Monolith NT.115 instrument (NanoTemper Technologies GmbH).

1) ASSAY and Drug Development Technologies AUGUST 2011