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Molecules 2013, 18(11), 13148-13174; doi:10.3390/molecules181113148
Review

Peptide Conjugation via CuAAC ‘Click’ Chemistry

1
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Received: 6 September 2013 / Revised: 9 October 2013 / Accepted: 10 October 2013 / Published: 24 October 2013
(This article belongs to the Special Issue Advances in Click Chemistry)
Download PDF [1173 KB, 18 June 2014; original version 18 June 2014]

Abstract

The copper (I)-catalyzed alkyne azide 1,3-dipolar cycloaddition (CuAAC) or ‘click’ reaction, is a highly versatile reaction that can be performed under a variety of reaction conditions including various solvents, a wide pH and temperature range, and using different copper sources, with or without additional ligands or reducing agents. This reaction is highly selective and can be performed in the presence of other functional moieties. The flexibility and selectivity has resulted in growing interest in the application of CuAAC in various fields. In this review, we briefly describe the importance of the structural folding of peptides and proteins and how the 1,4-disubstituted triazole product of the CuAAC reaction is a suitable isoster for an amide bond. However the major focus of the review is the application of this reaction to produce peptide conjugates for tagging and targeting purpose, linkers for multifunctional biomacromolecules, and reporter ions for peptide and protein analysis.
Keywords: CuAAC; click chemistry; chemical ligation; peptide ligation CuAAC; click chemistry; chemical ligation; peptide ligation
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.

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Ahmad Fuaad, A.A.H.; Azmi, F.; Skwarczynski, M.; Toth, I. Peptide Conjugation via CuAAC ‘Click’ Chemistry. Molecules 2013, 18, 13148-13174.

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