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.
| Original language | English |
|---|---|
| Journal | ChemBioChem |
| Volume | 20 |
| Issue number | 15 |
| Pages (from-to) | 1914-1918 |
| Number of pages | 5 |
| ISSN | 1439-4227 |
| DOIs | |
| Publication status | Published - 2019 |
Funding
M.R. and C.U. acknowledge the Deutsche Forschungsgemein-schaft (SPP1623) for financial support. M.R. is grateful to Rainer Winter for providing the CuI complex.
UN SDGs
This output contributes to the following UN Sustainable Development Goals (SDGs)
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SDG 3 Good Health and Well-being
Research Areas and Centers
- Academic Focus: Center for Brain, Behavior and Metabolism (CBBM)
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