Proteolysis targeting chimeras (PROTACs) are bivalent molecules that simultaneously bind to a chosen protein and E3 ubiquitin ligase, leading to the target protein’s degradation through the proteasome. Although there are multiple biophysical methods to screen ligands or characterize binary and ternary complexes, scientists face several challenges using these approaches, such as stability problems, difficulty evaluating binding events involving small molecules, and the large quantities of targets and ligands required. To overcome these obstacles, researchers look for a reliable, high throughput, and accurate method to assess PROTAC interactions.
Download this brochure from NanoTemper to learn about the advantages of employing their plate-based Dianthus platform for the mass-independent measurement of binding affinities in solution.
