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The biological activity of the glycoprotein hormone erythropoietin (EPO) is dependent mainly on the structure of its N‐linked glycans. We aimed to readily attach defined N‐glycans to EPO through copper‐catalyzed… Click to show full abstract
The biological activity of the glycoprotein hormone erythropoietin (EPO) is dependent mainly on the structure of its N‐linked glycans. We aimed to readily attach defined N‐glycans to EPO through copper‐catalyzed azide alkyne cycloaddition. EPO variants with an alkyne‐bearing non‐natural amino acid (Plk) at the N‐glycosylation sites 24, 38, and 83 were obtained by amber suppression followed by protein purification and refolding. Click conjugation of the alkynyl EPOs with biantennary N‐glycan azides provided biologically active site‐specifically modified EPO glycoconjugates.
Journal Title: ChemBioChem
Year Published: 2019
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