A new strategy for the chemoenzymatic synthesis of glycopeptides by De-O-acetylation with an esterase and glycosylations with glycosyltransferases
Authors: Japan Bioindustry Association, Advanced Industrial Science and Technology, Japan
- Deacetylation of glycopeptide with an esterase prevents base-induced side reactions, b-elimination, and epimerization
- An esterase from B. subtilis was utilized for Deacetylation of sugar hydroxyl groups on glycopeptide synthesis
- Deacetylation with an esterase and glycosylations with glycosyltransferases were accomplished in one-pot
Glycopeptides are fragments of glycoproteins and are important in evaluating the biological roles of carbohydrates in glycoproteins. Fmoc solid-phase peptide synthesis using acetyl-protected glycosylated amino acids is a common strategy for the preparation of glycopeptides, but this approach normally requires chemical de-O-acetylation with a base that β-eliminates sugar residues and epimerizes the peptide backbone. Here we demonstrate a facile new chemoenzymatic synthetic strategy for glycopeptides, using an esterase for the de-O-acetylation of sugar residues and glycosyltransferases for successive sugar elongations at neutral pH.
ESI-MS spectra were collected using an Advion expression Compact Mass Spectrometer (CMS) in negative ion mode.