ArticleChemical science2019
A synthetic approach to 'click' neoglycoprotein analogues of EPO employing one-pot native chemical ligation and CuAAC chemistry.
Article in Chemical science, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed, 15 citations in OpenAlex.
- Advances in the chemical synthesis of human proteoforms.Science China. Life sciences · 2025Review
- Expedient Azide-Alkyne Huisgen Cycloaddition Catalyzed by a Combination of VOSOACS organic & inorganic Au · 2024Article
- Chemical and Enzymatic Synthesis of Sialylated Glycoforms of Human Erythropoietin.Angewandte Chemie (International ed. in English) · 2021Article
- Recent Advances in the Chemical Biology ofMolecules (Basel, Switzerland) · 2021Review
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Authors and funding
5 authors at 1 institution in 1 country.
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Abstract
The clinical significance of batch-wise variability on the pharmacokinetics and potency of commercial erythropoietin (EPO), prepared recombinantly as a heterogeneous mixture of glycoforms, necessitates the development of synthetic strategies to afford homogenous EPO formulations. Herein we present a previously unexplored and divergent route towards 'click' neoglycoprotein analogues of EPO, employing one-pot native chemical ligation (NCL) of alkynylated peptides and copper-catalysed azide-alkyne cycloaddition (CuAAC) with azido monosaccharides. By design, our synthetic platform permits glycosylation at virtually any stage, providing flexibility for the synthesis of various glycoforms for biological analysis. Insights obtained from attempted folding of our 'click' neoglycoprotein EPO analogue, bearing four different neutral sugar moieties, highlight the important role played by the charged oligosaccharides present in native EPO glycoproteins.
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Registered trials
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