Publikation: Synthesis of Erythropoietins Site‐Specifically Conjugated with Complex‐Type N‐Glycans
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2019
Autor:innen
Boos, Irene
Jelkmann, Wolfgang
Unverzagt, Carlo
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ChemBioChem. Wiley. 2019, 20(15), pp. 1914-1918. ISSN 1439-4227. eISSN 1439-7633. Available under: doi: 10.1002/cbic.201900023
Zusammenfassung
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.
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Fachgebiet (DDC)
540 Chemie
Schlagwörter
Click chemistry, Glycoproteins, Protein Engineering, Protein modifications, synthetic glycans
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STREICHERT, Katharina, Carina SEITZ, Eugenia HOFFMANN, Irene BOOS, Wolfgang JELKMANN, Thomas BRUNNER, Carlo UNVERZAGT, Marina RUBINI, 2019. Synthesis of Erythropoietins Site‐Specifically Conjugated with Complex‐Type N‐Glycans. In: ChemBioChem. Wiley. 2019, 20(15), pp. 1914-1918. ISSN 1439-4227. eISSN 1439-7633. Available under: doi: 10.1002/cbic.201900023BibTex
@article{Streichert2019-08-01Synth-46286,
year={2019},
doi={10.1002/cbic.201900023},
title={Synthesis of Erythropoietins Site‐Specifically Conjugated with Complex‐Type N‐Glycans},
number={15},
volume={20},
issn={1439-4227},
journal={ChemBioChem},
pages={1914--1918},
author={Streichert, Katharina and Seitz, Carina and Hoffmann, Eugenia and Boos, Irene and Jelkmann, Wolfgang and Brunner, Thomas and Unverzagt, Carlo and Rubini, Marina}
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<dcterms:abstract xml:lang="eng">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.</dcterms:abstract>
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