A chemical strategy for protease substrate profiling

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UID: 11096

Author(s): Griswold, Andrew*, Bachovchin, Daniel* * MSK affiliated

Description: Here, we introduce a simple method, termed CHOPS, for the discovery of protease substrates. CHOPS exploits a 2-pyridinecarboxaldehyde (2PCA)-biotin probe, which selectively biotinylates protein N-termini except those with proline in the second position. CHOPS can, in theory, discover substrates for any protease, but is particularly well-suited to discover canonical DPP substrates, as cleaved but not intact DPP substrates can be identified by gel electrophoresis or mass spectrometry. This work delineates a practical technology for identifying protease substrates, which we anticipate will complement available “N-terminomic” approaches.

Subject of Study

Subject(s)

Access via PRIDE

Accession #: PXD013019
Access Restrictions: Free to All
Access Instructions: All public datasets available in PRIDE Archive in the repository can be accessed via the website by FTP link, Web Service (for programmatic access), and the PRIDE Inspector stand-alone tool.
Associated Publications: Griswold A, Cifani P, Rao S, Axelrod A, Miele M, Hendrickson R, Kentsis A, Bachovchin D. A chemical strategy for protease substrate profiling. Cell Chemical Biology. 2019; 26(6):901-907.e6.
Equipment Used: Q Exactive
Mass Spectrometer
Software Used: pFind 3
a computational solution for mass spectrometry-based proteomics
Dataset Format(s): FASTA, RAW, CFG
Dataset Size: 13.7 GB

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