Peptide Conjugation via CuAAC ‘Click’ Chemistry

Molecules

Abdullah A. H. Ahmad Fuaad¹  Fazren Azmi¹  Mariusz Skwarczynski¹ 

[1] School of Chemistry and Molecular Biosciences, University of Queensland, Brisbane, QLD 4072, Australia; E-Mails:

关键词: CuAAC;    click chemistry;    chemical ligation;    peptide ligation;   

DOI  :  10.3390/molecules181113148

来源: mdpi

【 摘 要 】

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.

【 授权许可】

CC BY   
© 2013 by the authors; licensee MDPI, Basel, Switzerland.