UNIT 21.22 Proteolytic Fingerprinting of Complex Biological Samples Using Combinatorial Libraries of Fluorogenic Probes
Published Online: 1 NOV 2012
Copyright © 2012 by John Wiley & Sons, Inc.
Lab Protocol Title
Current Protocols in Protein Science
How to Cite
Jambunathan, K., Watson, D. S., Kodukula, K. and Galande, A. K. 2012. Proteolytic Fingerprinting of Complex Biological Samples Using Combinatorial Libraries of Fluorogenic Probes. Current Protocols in Protein Science. 70:21.22.1–21.22.14.
- Published Online: 1 NOV 2012
- Published Print: NOV 2012
Proteases have garnered interest as candidate biomarkers and therapeutic targets for many human diseases. A key challenge is the identification and characterization of disease-relevant proteases in the complex milieu of biological fluids such as serum, plasma, and bronchoalveolar lavage, in which a multitude of hydrolases act in concert. This unit describes a protocol to map the global proteolytic substrate specificities of complex biological samples using a concise combinatorial library of internally quenched fluorogenic peptide probes (IQFPs). This substrate profiling approach provides a global and quantitative comparison of protease specificities between different biological samples. Such a comparative analysis can lead to the identification of disease-specific ‘fingerprints' of proteolytic activities with potential utility in diagnosis and therapy. Curr. Protoc. Protein Sci. 70:21.22.1-21.22.14. © 2012 by John Wiley & Sons, Inc.
- global proteolytic specificities;
- protease substrate identification