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Molecules 2013, 18(10), 12599-12608; doi:10.3390/molecules181012599

Comparative Analysis of Click Chemistry Mediated Activity-Based Protein Profiling in Cell Lysates

Lehrstuhl für Chemie der Biopolymere, Technische Universität München, Weihenstephaner Berg 3, 85354 Freising, Germany
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Received: 26 June 2013 / Revised: 7 August 2013 / Accepted: 26 September 2013 / Published: 11 October 2013
(This article belongs to the Special Issue Advances in Click Chemistry)
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Abstract

Activity-based protein profiling uses chemical probes that covalently attach to active enzyme targets. Probes with conventional tags have disadvantages, such as limited cell permeability or steric hindrance around the reactive group. A tandem labeling strategy with click chemistry is now widely used to study enzyme targets in situ and in vivo. Herein, the probes are reacted in live cells, whereas the ensuing detection by click chemistry takes place in cell lysates. We here make a comparison of the efficiency of the activity-based tandem labeling strategy by using Cu(I)-catalyzed and strain-promoted click chemistry, different ligands and different lysis conditions.
Keywords: activity-based probes; cathepsins; click chemistry; proteases; protein modification activity-based probes; cathepsins; click chemistry; proteases; protein modification
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This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

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MDPI and ACS Style

Yang, Y.; Yang, X.; Verhelst, S.H.L. Comparative Analysis of Click Chemistry Mediated Activity-Based Protein Profiling in Cell Lysates. Molecules 2013, 18, 12599-12608.

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