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

Katharina Streichert; Carina Seitz; Eugenia Hoffmann; Irene Boos; Wolfgang Jelkmann; Thomas Brunner; Carlo Unverzagt; Marina Rubini

doi:10.1002/cbic.201900023

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

Katharina Streichert, Carina Seitz, Eugenia Hoffmann, Irene Boos, Wolfgang Jelkmann, Thomas Brunner, Carlo Unverzagt, Marina Rubini^*

^*Corresponding author for this work

Institute of Physiology

4 Citations (Scopus)

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	https://doi.org/10.1002/cbic.201900023
Publication status	Published - 2019

Research Areas and Centers

Academic Focus: Center for Brain, Behavior and Metabolism (CBBM)

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

Access to Document

10.1002/cbic.201900023

Cite this

@article{b111733eef5d4523bab4a81d4a0e8cd2,

title = "Synthesis of Erythropoietins Site-Specifically Conjugated with Complex-Type N-Glycans",

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.",

author = "Katharina Streichert and Carina Seitz and Eugenia Hoffmann and Irene Boos and Wolfgang Jelkmann and Thomas Brunner and Carlo Unverzagt and Marina Rubini",

year = "2019",

doi = "10.1002/cbic.201900023",

language = "English",

volume = "20",

pages = "1914--1918",

journal = "Chembiochem",

issn = "1439-4227",

number = "15",

}

TY - JOUR

T1 - Synthesis of Erythropoietins Site-Specifically Conjugated with Complex-Type N-Glycans

AU - Streichert, Katharina

AU - Seitz, Carina

AU - Hoffmann, Eugenia

AU - Boos, Irene

AU - Jelkmann, Wolfgang

AU - Brunner, Thomas

AU - Unverzagt, Carlo

AU - Rubini, Marina

PY - 2019

Y1 - 2019

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=85068710231&partnerID=8YFLogxK

U2 - 10.1002/cbic.201900023

DO - 10.1002/cbic.201900023

M3 - Journal articles

C2 - 30973186

AN - SCOPUS:85068710231

SN - 1439-4227

VL - 20

SP - 1914

EP - 1918

JO - Chembiochem

JF - Chembiochem

IS - 15

ER -

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

Abstract

Research Areas and Centers

UN SDGs

Access to Document

Other files and links

Fingerprint

Cite this