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Applications of Copper-Catalyzed Click Chemistry in Activity-Based Protein Profiling

Department of Chemistry, Boston College, Chestnut Hill, MA 02467, USA
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Molecules 2014, 19(2), 1378-1393; https://doi.org/10.3390/molecules19021378
Received: 23 December 2013 / Revised: 9 January 2014 / Accepted: 17 January 2014 / Published: 27 January 2014
(This article belongs to the Special Issue Bioorthogonal Chemistry)
Activity-based protein profiling (ABPP) is a chemical proteomic technique that enables the interrogation of protein activity directly within complex proteomes. Given the dominant role of posttranslational modifications in regulating protein function in vivo, ABPP provides a direct readout of activity that is not attained through traditional proteomic methods. ABPP relies on the design of covalent binding probes that either target a specific enzyme or a class of enzymes with related function. These covalent warheads are coupled to either fluorophores or biotin groups for visualization and enrichment of these active proteins. The advent of bioorthogonal chemistries, in particular, the copper (I)-catalyzed azide-alkyne cycloaddition (CuAAC), has benefitted the field of ABPP by achieving the following: (1) replacing bulky reporter groups with smaller alkyne or azide groups to promote cell permeability; (2) adding modularity to the system such that a single probe can be diversified with a variety of reporter groups without the need to develop new synthetic routes; and (3) enabling the conjugation of complex linkers to facilitate quantitative proteomic analyses. Here, we summarize recent examples of CuAAC in ABPP that serve to illustrate the contribution of bioorthogonal chemistry to advancing discoveries in this field. View Full-Text
Keywords: click chemistry; activity-based protein profiling; bioorthogonal chemistry; azide-alkyne cycloaddition click chemistry; activity-based protein profiling; bioorthogonal chemistry; azide-alkyne cycloaddition
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Martell, J.; Weerapana, E. Applications of Copper-Catalyzed Click Chemistry in Activity-Based Protein Profiling. Molecules 2014, 19, 1378-1393.

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