Synthesis of Erythropoietins Site-Specifically Conjugated with Complex-Type N-Glycans

Katharina Streichert, Carina Seitz, Eugenia Hoffmann, Irene Boos, Wolfgang Jelkmann, Thomas Brunner, Carlo Unverzagt, Marina Rubini*

*Corresponding author for this work
4 Citations (Scopus)


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.

Original languageEnglish
Issue number15
Pages (from-to)1914-1918
Number of pages5
Publication statusPublished - 2019

Research Areas and Centers

  • Academic Focus: Center for Brain, Behavior and Metabolism (CBBM)


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