ArticleAngewandte Chemie (International ed. in English)2021
Chemical and Enzymatic Synthesis of Sialylated Glycoforms of Human Erythropoietin.
Article in Angewandte Chemie (International ed. in English), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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5 citing papers in PubMed, 23 citations in OpenAlex.
- Revealing the Biological Effect of theJournal of the American Chemical Society · 2026Article
- A Versatile Method for Site-Specific Chemical Installation of Aromatic Posttranslational Modification Analogs into Proteins.Journal of the American Chemical Society · 2024Article
- Semisynthesis of homogeneous spike RBD glycoforms from SARS-CoV-2 for profiling the correlations between glycan composition and function.National science review · 2024Article
- Total synthesis of interleukin-2Chemical science · 2023Article
- Chemical and Enzymatic Synthesis of Sialylated Glycoforms of Human Erythropoietin.Angewandte Chemie (International ed. in English) · 2021Article
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13 authors at 1 institution in 1 country.
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Abstract
Recombinant human erythropoietin (EPO) is the main therapeutic glycoprotein for the treatment of anemia in cancer and kidney patients. The in-vivo activity of EPO is carbohydrate-dependent with the number of sialic acid residues regulating its circulatory half-life. EPO carries three N-glycans and thus obtaining pure glycoforms provides a major challenge. We have developed a robust and reproducible chemoenzymatic approach to glycoforms of EPO with and without sialic acids. EPO was assembled by sequential native chemical ligation of two peptide and three glycopeptide segments. The glycopeptides were obtained by pseudoproline-assisted Lansbury aspartylation. Enzymatic introduction of the sialic acids was readily accomplished at the level of the glycopeptide segments but even more efficiently on the refolded glycoprotein. Biological recognition of the synthetic EPOs was shown by formation of 1:1 complexes with recombinant EPO receptor.
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