Label-free microscale thermophoresis discriminates sites and affinity of protein-ligand binding

Susanne A. I. Seidel, Dr. Christoph J. Wienken, Sandra Geissler, Dr. Moran Jerabek‐Willemsen, Dr. Stefan Duhr, Alwin Reiter, Prof. Dirk Trauner, Prof. Dieter Braun, Dr. Philipp Baaske

Angewandte Chemie
2012 vol: 51 issue: 42 pp: 10656-10659 doi: 10.1002/anie.201204268

Abstract

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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Topics: Analytical methods, Binding affinity, Label‐free methods, Protein conformation, Monolith – MicroScale Thermophoresis, MST, Proteins, Publications