Binding of the Geldanamycin Derivative 17-DMAG to Hsp90 Measured With the NanoTemper Monolith Technologies

This application note demonstrates the binding of the geldanamycin derivative 17-DMAG to Hsp90 using MicroScale Thermophoresis (MST). For proper folding, many proteins involved in signal-transduction pathways, cell-cycle regulation and apoptosis depend upon the ATP-dependent molecular chaperone Hsp90. Consequently Hsp90 turned out to be an attractive target for cancer therapeutics. The study shows that MST is capable of measuring interactions of small molecules with proteins. The high content information produced using the NanoTemper Monolith NT.115 and the Monolith NT-LabelFree allows direct adjustment and optimization of the assay conditions either by changing the type of capillaries or by adjusting the buffer conditions.