ENGase catalysed production of bioactive glycopeptides and glycoproteins
- Prof. Anthony Fairbanks (University of Canterbury)
- Tuesday 17 October 2017
2333 CC Leiden
The synthetic application of endo-β-N-acetylglucosaminidases (ENGases, e.g. Endo A, Endo M) promises to allow ready access to a wide variety of defined homogenous glycoproteins and glycopeptides.1 The use of N-glycans activated at the reducing terminus as oxazolines allows their high yielding attachment to almost any amino acid, peptide or protein that contains a GlcNAc residue as an acceptor. A wide variety of oxazoline donors is available, either by total synthesis or by isolation of the corresponding oligosaccharide from natural sources, and conversion to the oxazoline in water. The synthetic potential of these enzymes is augmented by the production of mutant glycosynthases. Their application for the production of glycosylated variants of the anti-diabetic peptide pramlintide, glycopeptide vaccines candidates with increased binding to APCs and phosphorylated glycoproteins will be discussed.
- Chem. Soc. Rev. 2017, 46, 5128 - 5146.