ArticleMethods in molecular biology (Clifton, N.J.)2023
Measuring the Interaction of Sterols and Steroids with Proteins by Microscale Thermophoresis.
Article in Methods in molecular biology (Clifton, N.J.), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed.
- Development of an EPR-based methodology to study protein-lipid interaction.Biophysical chemistry · 2026Article
- Binding of perilipin 3 to membranes containing diacylglycerol is mediated by conserved residues within its PAT domain.The Journal of biological chemistry · 2023Article
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Authors and funding
2 authors.
Funding
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Abstract
Determining the affinity and specificity of protein-lipid interactions is crucial for understanding the physiological function and mode of action of signaling lipids, including steroids. Here we describe a method that relies on microscale thermophoresis (MST) to monitor the binding of sterols and steroids to proteins. The protein of interest is expressed as a polyhistidine-tagged fusion in E. coli and purified by affinity chromatography on a nickel-based resin. The purified protein is then labeled with a fluorescent dye and incubated with a serial dilution of the lipid ligand. The protein-ligand interaction is monitored by MST, which detects the fraction of the protein bound to the ligand based on its altered mobility in a thermal gradient. A binding curve fitted to the measured data points is then used to calculate the corresponding dissociation constant.
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