Post-translational glycosylation introduces enormous structural and functional diversity into glycoproteins. O-linked glycoproteins are important in a variety of these processes. O-linked protein glycosylation can be divided into two general classes � those in which a GlcNAc residue is �-linked to the side chain of Ser/Thr, and those in which a GalNAc residue is a-O-linked to the side chain of Ser/Thr.  The latter is characteristic of mucins, O-glycosylated proteins comprising an important class of tumor-associated antigens that have received considerable attention in cancer vaccine therapies, whereas the former is found in the reversible modification of proteins, a process that is important for a variety of cellular processes. Epitope specific antibodies against both classes of O-linked glycoproteins are important tools for the study of their cellular functions, but O-linked glycopeptides often are only weakly immunogenic. In this presentation, orthogonal ligation techniques will be presented for the preparation of a-S-linked analogues that are metabilically more stable than O-linked peptides.1 In addition, enzymatic approaches will be presented for the preapration of �-S-linked glycopeptides.2,3References1. Galonic, D. P.; van der Donk, W.A.; Gin, D.Y. Oligosaccharide-peptide ligation of glycosyl thiolates with dehydropeptides.  Synthesis of S-linked mucin glycopeptide conjugates. Chem. Eur. J. 2003, 24, 5997-6006.2. Oman, T.J.; Boetcher, J.D.; Wang, H.; Okalibe, X.N.; van der Donk, W.A. Sublancin is not a Lantibiotic but an S-linked Glycopeptide. Nat. Chem. Biol. 2011, 2, 78-80.3. Wang, H.; van der Donk, W.A. Substrate selectivity of the S-glycosyltransferase from sublancin biosynthesis. J. Am. Chem.Soc. 2011 in press.

Chemical and enzymatic synthesis of <i>S</i>-linked glycopeptides

243rd National Meeting (2012)

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Chemical and enzymatic synthesis of S-linked glycopeptides