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.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1002/cbic.201900023 | DOI Listing |
Publication Analysis
Top Keywords
synthesis erythropoietins
4
erythropoietins site-specifically
4
site-specifically conjugated
4
conjugated complex-type
4
complex-type n-glycans
4
n-glycans biological
4
biological activity
4
activity glycoprotein
4
glycoprotein hormone
4
hormone erythropoietin
4
Similar Publications
Want AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!