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Related Experiment Video

Updated: Jan 26, 2026

Sigma's Non-specific Protease Activity Assay - Casein as a Substrate

Sigma's Non-specific Protease Activity Assay - Casein as a Substrate

Published on: September 17, 2008

A Chemical Strategy for Protease Substrate Profiling.

Andrew R Griswold¹, Paolo Cifani², Sahana D Rao³

¹Weill Cornell/Rockefeller/Sloan Kettering Tri-Institutional MD-PhD Program, New York, NY 10065, USA; Pharmacology Program, Weill Cornell Graduate School of Medical Sciences, Memorial Sloan Kettering Cancer Center, New York, NY 10065, USA.

Cell Chemical Biology

|April 23, 2019

Summary

This summary is machine-generated.

Researchers developed CHOPS, a new method for discovering protease substrates. This technique helps identify dipeptidyl peptidase (DPP) substrates, revealing DPP8 and DPP9 do not directly cleave Nlrp1.

Keywords:

N-terminal modification Nlrp1 inflammasome chemical probes mass spectrometry-based proteomics protease substrates

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Area of Science:

Biochemistry
Proteomics
Enzymology

Background:

Dipeptidyl peptidases (DPPs) are crucial enzymes regulating bioactive peptides.
Identifying DPP substrates is challenging due to technical limitations.
Understanding DPP function requires effective substrate discovery methods.

Purpose of the Study:

To introduce a novel chemical enrichment method (CHOPS) for protease substrate discovery.
To apply CHOPS for identifying substrates of dipeptidyl peptidases (DPPs).
To investigate the interaction between DPP8/DPP9 and the Nlrp1 inflammasome.

Main Methods:

Development of CHOPS utilizing a 2-pyridinecarboxaldehyde (2PCA)-biotin probe.
Selective biotinylation of protein N-termini, excluding those with proline at the second position.
Analysis of cleaved vs. intact substrates via gel electrophoresis and mass spectrometry.

Main Results:

CHOPS successfully enables the discovery of protease substrates, particularly for DPPs.
DPP8 and DPP9 were found not to directly cleave the Nlrp1 inflammasome component.
DPP9 efficiently cleaves short peptides but not full-length proteins.

Conclusions:

CHOPS provides a practical and versatile technology for identifying protease substrates.
The findings offer new insights into the regulatory mechanisms of the Nlrp1 inflammasome.
This method is expected to complement existing N-terminomic approaches in proteomics.