Synthesis of Erythropoietins Site‐Specifically Conjugated with Complex‐Type N‐Glycans

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2019
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Boos, Irene
Jelkmann, Wolfgang
Unverzagt, Carlo
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urn:nbn:de:bsz:352-2-1k6u2xu7jov4m7
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10.1002/cbic.201900023
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ChemBioChem ; 20 (2019), 15. - pp. 1914-1918. - Wiley. - ISSN 1439-4227. - eISSN 1439-7633
Abstract
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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540 Chemistry
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Click chemistry, Glycoproteins, Protein Engineering, Protein modifications, synthetic glycans
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ISO 690STREICHERT, 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. 20(15), pp. 1914-1918. ISSN 1439-4227. eISSN 1439-7633. Available under: doi: 10.1002/cbic.201900023
BibTex
@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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