Abstract
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.

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