ArticleProtein science : a publication of the Protein Society2025
Unlocking GPCR-ligand interactions: Measuring binding affinities with thermal shift assay.
Article in Protein science : a publication of the Protein Society, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- Article
- Detection of an Antagonist Bound to the Neurokinin a Receptor in Styrene-Maleic Acid Lipid Particles byChembiochem : a European journal of chemical biology · 2026Article
- Unlocking GPCR-ligand interactions: Measuring binding affinities with thermal shift assay.Protein science : a publication of the Protein Society · 2025Article
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12 authors.
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Abstract
G protein-coupled receptors (GPCRs) constitute the largest transmembrane protein superfamily, with over 800 representatives in the human genome. Recognized as pivotal targets in pharmacological research and drug discovery, these receptors play a crucial role in advancing therapeutics. Understanding the molecular mechanisms of receptor-ligand interactions is imperative for drug discovery applications. However, experimental procedures for measuring ligand binding are complicated by various factors, including the transmembrane nature of the receptors and the high cost associated with specialized instruments and consumables. Here we introduce an application of the thermal shift assay (TSA) to measuring ligand binding affinities for GPCRs. TSA is a cost-effective and user-friendly method that detects changes in protein stability induced by alterations in environmental conditions. Employing the human A
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