2019-08-01, Streichert, Katharina, Seitz, Carina, Hoffmann, Eugenia, Boos, Irene, Jelkmann, Wolfgang, Brunner, Thomas, Unverzagt, Carlo, Rubini, Marina

The biological activity of glycoprotein hormone erythropoietin (EPO) is dependent mainly on the structure of its N-linked glycans. We aimed at readily attaching N-glycans to EPO via defined alkyne groups. EPO variants with an alkyne bearing amino acid (Plk) at the N-glycosylation sites 24, 38 and 83 were obtained by amber suppression followed by refolding. Click-conjugation of the alkinyl EPOs with biantennary N-glycan azides provided biologically active site-specifically modified EPO glycoconjugates.