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Synthesis of Erythropoietins Site‐Specifically Conjugated with Complex‐Type N ‐Glycans
Author(s) -
Streichert Katharina,
Seitz Carina,
Hoffmann Eugenia,
Boos Irene,
Jelkmann Wolfgang,
Brunner Thomas,
Unverzagt Carlo,
Rubini Marina
Publication year - 2019
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201900023
Subject(s) - glycoconjugate , glycan , glycosylation , alkyne , chemistry , azide , glycoprotein , click chemistry , erythropoietin , biochemistry , biological activity , cycloaddition , conjugated system , combinatorial chemistry , catalysis , biology , organic chemistry , in vitro , polymer , endocrinology
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.
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