ArticleScientific reports2018
Near-native, site-specific and purification-free protein labeling for quantitative protein interaction analysis by MicroScale Thermophoresis.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed.
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- Microscale Thermophoresis Analysis of Chromatin Interactions.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Discovery of Inhibitory Fragments That Selectively Target Spire2-FMN2 Interaction.Journal of medicinal chemistry · 2023Article
- Phosphoglycerate kinase is a central leverage point in Parkinson's Disease driven neuronal metabolic deficits.bioRxiv : the preprint server for biology · 2023Article
- Non-covalent dyes in microscale thermophoresis for studying RNA ligand interactions and modifications.Chemical science · 2023Article
- Exploring the Binding Affinity of the ARR2 GARP DNA Binding Domain via Comparative Methods.Genes · 2023Article
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- Discovery of New Zika Protease and Polymerase Inhibitors through the Open Science Collaboration Project OpenZika.Journal of chemical information and modeling · 2022Article
- An Optimized Microscale Thermophoresis Method for High-Throughput Screening of DNA Methyltransferase 2 Ligands.ACS pharmacology & translational science · 2022Article
- Essential role of Wtip in mouse development and maintenance of the glomerular filtration barrier.American journal of physiology. Renal physiology · 2022Article
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12 authors.
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Abstract
MicroScale Thermophoresis (MST) is a frequently used method for the quantitative characterization of intermolecular interactions with several advantages over other technologies. One of these is its capability to determine equilibrium constants in solution including complex biological matrices such as cell lysates. MST requires one binding partner to be fluorescent, which is typically achieved by labeling target proteins with a suitable fluorophore. Here, we present a near-native, site-specific in situ labeling strategy for MST experiments that enables reliable measurements in cell lysates and that has distinct advantages over routine covalent labeling techniques. To this end, we exploited the high-affinity interaction of tris-NTA with oligohistidine-tags, which are popular for purification, immobilization or detection of recombinant proteins. We used various DYE-tris-NTA conjugates to successfully label His-tagged proteins that were either purified or a component of cell lysate. The RED-tris-NTA was identified as the optimal dye conjugate with a high affinity towards oligohistidine-tags, a high fluorescence signal and an optimal signal-to-noise ratio in MST binding experiments. Owing to its emission in the red region of the spectrum, it also enables reliable measurements in complex biological matrices such as cell lysates allowing a more physiologically realistic assessment and eliminating the need for protein purification.
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