In mammalian glycomes, O-glycans and O-glycopeptides/glycoproteins compose an indispensable category. These O-glycans are linked to peptides/proteins via Ser/Thr. Although functional important, the synthesis of such O-glycans/glycopeptides/glycoproteins is still lagging behind, hindering further functional study. By a core synthesis – enzymatic extension (CSEE) strategy, we achieved the complexity and diversity of O-glycans/glycopeptides/glycoproteins with most natural structural diversity. Starting with 8 chemically prepared O-GalNAc core structures and 2 O-Man cores, we diversified the glycans with specific glycosyltransferases to over 100 O-GalNAc glycans and over 40 O-Man glycans, which is by far the most complex O-glycan library. For O-glycopeptide/glycoprotein synthesis, the chemically prepared core glycans were incorporated into glycopepride/glycoprotein by solid-phase peptide synthesis, and the glycans were further extended to provide fully glycosylated O-glycopeptides/glycoproteins. The O-glycans and the O-glycopeptides/glycoproteins prepared by this strategy should serve as standard for O-glycan structure characterization and are valuable for functional glycomic studies to better understand the functions and mechanisms of O-glycans as well as O-glycopeptides/glycoproteins.

Production of O-glycans and O-glycopeptides/glycoproteins by chemical and enzymatic catalysis production of O-glycans and O-glycopeptides/glycoproteins by chemical and enzymatic catalysis

255th National Meeting (2018)

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