Journal of the American Chemical Society · 2009 · 65 citations · 14 references
Life SciencesBiochemistryMolecular BiologyBiocatalysisEnzymologyGlycobiologyGlycan BiosynthesisGlycan-protein InteractionsPeptide Bond ChemistryPeptide ChemistryProtein GlycosylationProtein SortingChemoenzymatic Glycan SynthesisGlycine ConjugationGlycopeptide AnalysisGlycopeptide SynthesisGlycophosphatidylinositol-anchored ProteinsPeptide ConjugatesPeptide Coupling ReactionsPeptide Coupling Reagents
It is demonstrated that sortase A (SrtA) can catalyze efficient coupling of peptides to GPI analogues with a glycine residue attached to the phosphoethanolamine moiety at the nonreducing end to form GPI-linked peptides. This represents the first chemoenzymatic synthesis of GPI-peptide conjugates and is a proof-of-concept for the potential application of SrtA to the synthesis of more complex GPI-anchored peptides/glycopeptides and GPI-anchored proteins/glycoproteins.
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