Angewandte Chemie International Edition · 2008 · 140 citations · 26 references
Life SciencesBiochemistryMolecular BiologyCarbohydrate ChemistryGlycobiologyProtein BiochemistryGlycan BiosynthesisGlycan StructureGlycan-protein InteractionsN-linked GlycosylationO-linked GlycosylationProtein GlycosylationLectin Binding SpecificityLectin InteractionsLectin-carbohydrate InteractionsLectin-carbohydrate RecognitionLectinsO-linked N-acetylglucosamine ModificationProtein Glycosylation Analysis
Changing employment: Receptor 1 binds beta-N-acetylglucosaminyl (beta-GlcNAc) up to 100 times more strongly than it does glucose. This synthetic lectin shows affinities similar to wheat germ agglutinin (WGA), a natural lectin used to bind GlcNAc. Remarkably, 1 is more selective than WGA. It favors especially the glycoside unit in glycopeptide 2, a model of the serine-O-GlcNAc posttranslational protein modification.
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