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Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies
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Cleavable Linkers in Chemical Proteomics Applications.

Yinliang Yang1, Marko Fonović2, Steven H L Verhelst3,4

  • 1Lehrstuhl für Chemie der Biopolymere, Technische Universität München, Weihenstephaner Berg 3, 85354, Freising, Germany.

Methods in Molecular Biology (Clifton, N.J.)
|October 26, 2016
PubMed
Summary

Identifying protein targets of small molecule probes is key in chemical biology. This chapter reviews cleavable linkers used in mass spectrometry-based proteomics for improved protein identification.

Keywords:
Activity-based probesChemical proteomicsCleavable linkersClick chemistryEnrichmentMass spectrometryProtein identificationTarget discovery

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Area of Science:

  • Chemical Biology
  • Proteomics

Background:

  • Activity-based protein profiling (ABPP) and chemical biology rely on identifying protein targets of small molecule probes.
  • Mass spectrometry (MS) is the standard technique for protein target identification.

Purpose of the Study:

  • To provide an overview of cleavable linkers used in chemical proteomics.
  • To discuss the diverse chemistries of these linkers.
  • To explain how cleavable linkers enhance protein identification.

Main Methods:

  • Review of literature on cleavable linkers in chemical proteomics.
  • Discussion of linker chemistries and their application in MS-based protein identification.

Main Results:

  • Cleavable linkers are increasingly utilized in ABPP strategies.
  • Various linker chemistries offer distinct advantages for protein enrichment and identification.
  • These linkers significantly facilitate the identification of small molecule protein targets.

Conclusions:

  • Cleavable linkers are essential tools in modern chemical proteomics.
  • Understanding linker chemistry is crucial for optimizing target identification workflows.
  • The strategic use of cleavable linkers advances the field of chemical biology.