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Updated: May 18, 2026

Use of Microscale Thermophoresis to Measure Protein-Lipid Interactions
Published on: February 10, 2022
Label-free microscale thermophoresis discriminates sites and affinity of protein-ligand binding
Susanne A I Seidel1, Christoph J Wienken, Sandra Geissler
1Systems Biophysics and Functional Nanosystems, Ludwig-Maximilians-Universität München, Amalienstrasse 54, 80799 Munich, Germany.
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 Ca(2+) ions to synaptotagmin was quantified.
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