Probing glycans with the copper(I)-catalyzed [3+2] azide-alkyne cycloaddition

The imposing structural complexity and heterogeneity of glycans has made the study of their precise biological roles challenging. However, recently developed synthetic and screening techniques have enabled the study of many aspects of glycan activity that were previously inaccessible. Among these new methods, the Copper(I)-catalyzed Azide-Alkyne [3+2] Cycloaddition (CuAAC) has provided a means to mimic multivalent glycan display, manipulate cellular glycans in vivo for visualization and isolation, and generate useful inhibitors of glycoprotein processing.