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Pharmaceuticals 2018, 11(2), 49; https://doi.org/10.3390/ph11020049

A Short Peptide Inhibitor as an Activity-Based Probe for Matriptase-2

Pharmaceutical Chemistry I, Pharmaceutical Institute, University of Bonn, Bonn 53113, Germany
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Received: 30 April 2018 / Revised: 15 May 2018 / Accepted: 17 May 2018 / Published: 21 May 2018
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Abstract

Matriptase-2 is a type II transmembrane serine protease and a key regulator of systemic iron homeostasis. Since the activation mechanism and several features of the physiological role of matriptase-2 are not fully understood, there is strong need for analytical tools to perform tasks such as distinguishing active and inactive matriptase-2. For this purpose we present a short biotinylated peptide derivative with a chloromethyl ketone group, biotin-RQRR-CMK, as an activity-based probe for matriptase-2. Biotin-RQRR-CMK was kinetically characterized and exhibited a second-order rate constant of inactivation (kinac/Ki) of 10,800 M−1 s−1 towards the matriptase-2 activity in the supernatant of transfected human embryonic kidney (HEK) cells. Biotin-RQRR-CMK was able to label active matriptase-2, as visualized in western blot experiments. Pretreatment with aprotinin, an active-site directed inhibitor of serine proteases, protected matriptase-2 from the reaction with biotin-RQRR-CMK. View Full-Text
Keywords: matriptase-2; Activity-based probe; peptide inhibitor matriptase-2; Activity-based probe; peptide inhibitor
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).
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Mangold, M.; Gütschow, M.; Stirnberg, M. A Short Peptide Inhibitor as an Activity-Based Probe for Matriptase-2. Pharmaceuticals 2018, 11, 49.

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