All biomolecules operate and interact in aqueous solutions, surrounded by a characteristic hydration shell. Virtually any conformational change of a biomolecule, e.g. the formation of a protein-protein complex or the binding of a small molecule, results in a change of the individual hydration shell.
A German company called NanoTemper Technologies has found a way to easily monitor these specific changes in the hydration shell and to derive quantitative information on interactions, conformational changes and macromolecular stability. The beauty of the concept termed Microscale Thermophoresis (MST) lies in its ability to observe and measure various parameters, such as affinities and binding energetics, at conditions which almost fully mirror the native environment of the biomolecules found in cells.
This is of great value, in particular for interactions that are difficult to access with standard methods, like the binding of small molecules or single ions to larger components of the cell, or the interactions of peptides and proteins to membrane receptors, the most important pharmaceutical drug targets.
NanoTemper, a spin-off from the Center of NanoScience (CeNS) at Ludwig-Maximilians-University in Munich (Germany), was founded in 2008. The company is headquartered in Munich and runs a fully owned subsidiary in San Francisco (USA). NanoTemper offers instruments and consumables to customers worldwide. The products provide scientists in basic research with cost-effective access to an enabling technology and allow experiments that have never been possible before. Pharmaceutical and biotech companies can use the technology for faster and better characterization of drug candidates. For more information visit www.nanotemper.de.
Pictured below: Monolith NT.115, one of NanoTemper´s Microscale Thermophoresis instruments