FRISBI
Microscale Thermophoresis (MST) is a powerful innovative technology to characterize biomolecular interactions. It detects changes in the hydration shell of molecules and measures biomolecule interactions under close-to-native conditions: immobilization-free and in any bioliquids of choice. This technology has several advantages over other standard techniques to analyze interactions, such as surface plasmon resonance (SPR) and isothermal microcalorimetry (ITC). It can measure affinities in free solution without surface immobilization with low sample consumption and within sub-nM to mM range. MST is also applicable to a wide size range of biomolecules (ions, proteins,…) and experiments can be carried out with a broad range of solution conditions, including detergent mixtures.
Infrared-lasers are used to achieve precise microscale temperature gradients within thin glass capillaries that are filled with a solution of choice (buffer or serum, cell lysate and other bioliquids). Molecules move along these temperature gradients. Any change of the hydration shell of biomolecules due to changes in their primary, secondary, tertiary and/or quaternary structure affects the thermophoretic movement and is used to determine binding affinities with high accuracy and sensitivity.
The NanoTemper´s Monolith platform provides instruments, consumables and reagents for analyzing biomolecule interactions with fluorescence and label-free. It utilizes Microscale Thermophoresis to enable real-time, immobilization free analysis of biomolecules providing information on the affinity, stoichiometry and aggregation properties of biomolecules in buffers and complex biological liquids including blood serum and cell lysate.
For more information see http://www.afmb.univ-mrs.fr/en/facility/structural-biology/biophysical-techniques/