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Peptide Conjugation via CuAAC ‘Click’ Chemistry
School of Chemistry and Molecular Biosciences, University of Queensland, Brisbane, QLD 4072, Australia
School of Pharmacy, University of Queensland, Woolloongabba, QLD 4012, Australia
* Author to whom correspondence should be addressed.
Received: 6 September 2013; in revised form: 9 October 2013 / Accepted: 10 October 2013 / Published: 24 October 2013
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
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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.
Ahmad Fuaad AAH, Azmi F, Skwarczynski M, Toth I. Peptide Conjugation via CuAAC ‘Click’ Chemistry. Molecules. 2013; 18(11):13148-13174.
Ahmad Fuaad, Abdullah A.H.; Azmi, Fazren; Skwarczynski, Mariusz; Toth, Istvan. 2013. "Peptide Conjugation via CuAAC ‘Click’ Chemistry." Molecules 18, no. 11: 13148-13174.