Journal article

Authors list: Pollaro, L; Diderich, P; Angelini, A; Bellotto, S; Wegner, H; Heinis, C

Publication year: 2012

Pages: 18-20

Journal: Analytical Biochemistry

Volume number: 427

Issue number: 1

ISSN: 0003-2697

DOI Link: https://doi.org/10.1016/j.ab.2012.04.025

Publisher: Elsevier

Abstract: 
The measurement of activities from individual proteases in biological samples is difficult because of the numerous proteases, their overlapping activities, and the lack of specific substrates. We applied selective protease inhibitors based on bicyclic peptides (>2000-fold selective over related proteases) to block individual proteases, allowing the quantification of their net activities. In protease mixtures, activity contributions of the serine proteases plasma kallikrein and urokinase-type plasminogen activator (uPA) were accurately quantified. In a tumor extract, we could quantify uPA activity. Because bicyclic peptide inhibitors toward virtually any protease can be generated by phage display, the approach should be applicable to any protease.

Harvard Citation style: Pollaro, L., Diderich, P., Angelini, A., Bellotto, S., Wegner, H. and Heinis, C. (2012) Measuring net protease activities in biological samples using selective peptidic inhibitors, Analytical Biochemistry, 427(1), pp. 18-20. https://doi.org/10.1016/j.ab.2012.04.025

APA Citation style: Pollaro, L., Diderich, P., Angelini, A., Bellotto, S., Wegner, H., & Heinis, C. (2012). Measuring net protease activities in biological samples using selective peptidic inhibitors. Analytical Biochemistry. 427(1), 18-20. https://doi.org/10.1016/j.ab.2012.04.025