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Mass spectrometry-assisted protease substrate screening.

Hartmut Schlüter¹, Jana Rykl, Joachim Thiemann

¹Med. Clinic IV, Nephrology, Campus Benjamin Franklin, Charité-University Medicine Berlin, Hindenburgdamm 30, 12200 Berlin, Germany. Hartmut.schlueter@charite.de

Analytical Chemistry

|February 1, 2007

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Researchers developed a new assay to identify unknown protease substrates in the human body. This method uses immobilized proteins and mass spectrometry to find natural substrates for proteases, aiding in understanding their physiological roles.

Area of Science:

Biochemistry
Proteomics
Molecular Biology

Background:

Over 500 human protease genes are known, but their endogenous substrates are largely unidentified.
Identifying protease substrates is crucial for understanding protease physiological roles.

Purpose of the Study:

To present a novel, automatable assay for identifying endogenous protease substrates.
To demonstrate the assay's efficacy in identifying thrombin substrates in human plasma.

Main Methods:

Incubation of immobilized protein fractions with a defined protease.
Concentration of released peptides via reversed-phase chromatography.
Analysis of peptides using tandem mass spectrometry and database searching.

Main Results:

Related Experiment Videos

The assay successfully identified fibrinopeptides released from fibrinogen by thrombin.
This demonstrates the method's capability to pinpoint natural substrates.

Conclusions:

The developed assay is effective for identifying endogenous protease substrates.
This technique facilitates the discovery of unknown protease functions.