Solid-phase synthesis of O-mannosylated peptides: two strategies compared.
A comparison of the O-glycosylation of resin-bound assembled peptides with the incorporation of glycosylated amino acids using established chemistry is presented. Fmoc/tert-butyl-based protecting groups were used for the peptidic moieties in conjunction with acetyl sugar protection. Koenigs-Knorr glycosylations were carried out using protected bromomannose derivatives, the acceptor being threonine or serine, either in solution or within a resin-bound peptide. The characterisation of microgram quantities of glycopeptides by the use of glycosidases in combination with mass spectrometry is also described.
Andrews
D M
DM
Glaxo Group Research, Greenford, Middlesex, UK.
Seale
P W
PW
D000595:Amino Acid Sequence; D001577:Benzophenones / Q000737:chemistry; D006020:Glycopeptides / Q000138:chemical synthesis* / Q000378:metabolism; D006031:Glycosylation; D009682:Magnetic Resonance Spectroscopy; D008358:Mannose / Q000737:chemistry; D008361:Mannosidases / Q000378:metabolism; D008362:Mannosides / Q000138:chemical synthesis* / Q000378:metabolism; D008969:Molecular Sequence Data; D012545:Schiff Bases / Q000737:chemistry; D016339:Spectrometry, Mass, Fast Atom Bombardment; D043323:alpha-Mannosidase
D001577:Benzophenones; D006020:Glycopeptides; D008362:Mannosides; D012545:Schiff Bases; D008361:Mannosidases; D043323:alpha-Mannosidase; D008358:Mannose