• Open Access

Label-Free Microscale Thermophoresis Discriminates Sites and Affinity of Protein–Ligand Binding

Authors


  • We thank the Nanosystems Initiative Munich (NIM) and the Zentrales Innovationsprogramm Mittelstand (ZIM) for financial support of this research. This work was supported by the Federal Ministry of Education and Research (Germany), the Center for NanoScience (CeNS), Center for Integrated Protein Science Munich (CIPSM), and a joint grant from the Deutsche Forschungsgemeinschaft (DFG) and FOR 1279 (Protein Switches as Optogenetic Tools)..

Abstract

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Look, no label! Microscale thermophoresis makes use of the intrinsic fluorescence of proteins to quantify the binding affinities of ligands and discriminate between binding sites. This method is suitable for studying binding interactions of very small amounts of protein in solution. The binding of ligands to iGluR membrane receptors, small-molecule inhibitorss to kinase p38, aptamers to thrombin, and Ca2+ ions to synaptotagmin was quantified.

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