Oligosaccharides of protein surface play important roles in many biological events. In order to evaluate the function of oligosaccharides dependent on glycosylation positions and glycosylation number, we need efficient synthetic methods of glycoproteins having homogeneous oligosaccharides.1
In order to prepare homogeneous glycoproteins, we have studied the efficient semisynthetic method of peptide-thioester. Using long peptides prepared in E. Coli, we have studied the thioesterification of the peptide by the activation of a cysteine residue intentionally incorporated at the C-terminal.2-3 Thus we found that three types of thioesterification methods and these methods efficiently gave peptide-thioesters in moderate yield.
In terms of coupling reaction of glycosyl-amino acid and peptide-thioester, we developed amino thioacid method.4 The coupling of a peptide-thioester with a glycosyl-amino thioacid efficiently yielded a peptide having glycosyl-amino thioacid at the C-terminal. Toward this glycopeptide-thioacid, ligation5 with a peptide having a cysteine at the N-terminal was performed in order to synthesize a target glycoprotein.
In this presentation, I would discuss a new semi-synthetic method of glycoproteins.