For many eukaryotic proteins, processing by post-translational modifications such as glycosylation is a critical step for correct folding and achievement of biological activity. These modifications that occur naturally within eukaryotic cells have to be replicated when preparing peptides and proteins that are chemically synthesized or recombinantly-produced in prokaryotic cells.
This technology enables production of glycosylated peptides using a new, patented method relying on a two-step procedure involving reversibly conjugating a peptide with a hydrophilic polymer such as PEG; and subsequently glycosylating the polymer-conjugated peptide using glycosyltransferases.