Can GST Pull-Down Assays Be Applied to Analyze Interactions Between Proteins and Small-Molecule Compounds?

GST pull-down assays are widely used for analyzing protein–protein interactions. In this technique, a GST-tagged bait protein is employed to capture binding partners from a complex mixture via affinity to glutathione beads, followed by enrichment and detection using methods such as SDS-PAGE and Western blotting.

 

While traditionally applied to study interactions between two proteins, the GST pull-down approach can also be adapted to investigate interactions between a protein and a small-molecule compound. This application is commonly associated with fields such as chemical proteomics or small-molecule affinity purification.

 

Similar to protein-based pull-downs, chemical proteomics and small-molecule affinity approaches rely on affinity-based capture of protein targets through specific interactions with immobilized small molecules or tagged compounds. These techniques are particularly valuable for exploring protein–small molecule interactions, drug–target binding events, and the identification of novel drug targets.

 

Therefore, GST pull-down assays can indeed be utilized to study interactions between a protein and a small molecule, provided that appropriate affinity tags or chemical conjugates are used for the enrichment and detection steps.

 

MtoZ Biolabs, an integrated chromatography and mass spectrometry (MS) services provider.

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