ArticleAngewandte Chemie (International ed. in English)2022
Semisynthesis of Homogeneous, Active Granulocyte Colony-Stimulating Factor Glycoforms.
Article in Angewandte Chemie (International ed. in English), 2022. 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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Who cites it
5 citing papers in PubMed.
- Chemical synthesis uncovers the significant impact of natural glycosylation on islet amyloid polypeptide aggregation.Science advances · 2025Article
- Chemical Synthesis of Human Proteoforms and Application in Biomedicine.ACS central science · 2024Review
- Enhanced native chemical ligation by peptide conjugation in trifluoroacetic acid.Science advances · 2024Article
- Light-Cleavable Auxiliary for Diselenide-Selenoester Ligations of Peptides and Proteins.Chemistry (Weinheim an der Bergstrasse, Germany) · 2023Article
- Semisynthesis of Homogeneous, Active Granulocyte Colony-Stimulating Factor Glycoforms.Angewandte Chemie (International ed. in English) · 2022Article
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Granulocyte colony stimulating factor (G-CSF) is a cytokine used to treat neutropenia. Different glycosylated and non-glycosylated variants of G-CSF for therapeutic application are currently generated by recombinant expression. Here, we describe our approaches to establish a first semisynthesis strategy to access the aglycone and O-glycoforms of G-CSF, thereby enabling the preparation of selectively and homogeneously post-translationally modified variants of this important cytokine. Eventually, we succeeded by combining selenocysteine ligation of a recombinantly produced N-terminal segment with a synthetic C-terminal part, transiently equipped with a side-chain-linked, photocleavable PEG moiety, at low concentration. The transient PEGylation enabled quantitative enzymatic elongation of the carbohydrate at Thr133. Overall, we were able to significantly reduce the problems related to the low solubility and the tendency to aggregate of the two protein segments, which allowed the preparation of four G-CSF variants that were successfully folded and demonstrated biological activity in cell proliferation assays.
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