Chemoenzymatic synthesis of sulfated O-glycopeptides from human CD34.

O-Glycosylation is a key modulator of CD34 biofunction. To investigate the distinct roles of different glycoform modifications, we report an efficient chemoenzymatic strategy to rapidly assemble a library of CD34 O-glycopeptides bearing sulfated and sialylated glycan variants, enabling the elucidation of how specific glycan modifications govern molecular recognition events.