ArticleRapid communications in mass spectrometry : RCM2023
Native mass spectrometry interrogation of complexes formed during targeted protein degradation.
Article in Rapid communications in mass spectrometry : RCM, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed, 9 citations in OpenAlex.
- Interface Architecture of a VHL-PROTAC Complex with and without Cullin-2.Journal of the American Chemical Society · 2026Article
- Solution characterization of TraW, a regulatory protein of the F plasmid type 4 secretion system.Structural dynamics (Melville, N.Y.) · 2026Article
- Traversing the drug discovery landscape using native mass spectrometry.Current opinion in structural biology · 2025Review
- Native mass spectrometry interrogation of complexes formed during targeted protein degradation.Rapid communications in mass spectrometry : RCM · 2023Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
rationaleProtein degraders are small molecules that promote cellular degradation of a target protein. Degraders simultaneously bind to their target and an E3 ligase, bringing them into close spatial proximity, but the formation of this ternary complex is difficult to measure with many biophysical techniques.
methodsNative mass spectrometry (nMS) is an effective label-free technique to identify the complexes formed by proteolysis-targeting chimeras (PROTACs). It can monitor the formation of ternary E3-PROTAC-target complexes and detect intermediate binary species. Experiments are described using a Synapt G2Si (Waters) equipped with a nano-electrospray ionisation source.
resultsThe protocol describes nMS experiments for measuring the complexes formed by PROTAC molecules. It also describes how to investigate differences in the affinity of PROTAC complexes, whether a PROTAC shows specificity for a given target and whether a PROTAC shows cooperative behaviour.
conclusionsHere, we provide step-by-step instructions for the sample preparation of PROTAC complexes and their nMS interrogation to obtain optimal information on their binding modes.
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