Glycoprotein plays an important role in a multitude of biological processes such as cell–cell recognition, growth, differentiation, and cell death. It has been shown that specific glycosylation changes are key in disease progression and can have diagnostic value for a variety of disease types such as cancer and inflammation.  A need in new strategies for the selective isolation of glycoproteins from complicated biological samples is in high demand. TO this end, recently,  a synthetic chemical probe composed of boronic acid as an affinity ligand and reactive tosyl group, BA-tosyl molecule, has been successfully developed. The boronic acid is a major component acting as an affinity head to direct the formation of a boronate diester ring with the diol group of glycans . The proximity effect would then trigger  an SN2 reaction with the nucleophilic residues of the boronated glycoproteins to the reactive tosyl group and covalently transfer a tag molecule to the targeted glycoprotein with an ether linkage.

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

Furthermore, the strain promoted alkyne cycloaddition (SPAAC) has been further applied inthe fabrication of glycoprotein microarray which can prevent using the Cu catalysts. To this purpose, the surface blocking and conjugation have been carefully studied. We believed that this newly developed method would greatly accelerate the understanding of glycoproteins and their interactions with other biomacromolecules.