Journal
BIOCONJUGATE CHEMISTRY
Volume 27, Issue 9, Pages 1972-1975Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.bioconjchem.6b00385
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Funding
- National Basic Research Program of China (973 Program) [2012CB910300]
- National Natural Science Foundation of China [30970644, 31000371]
- National Institute of Health [R01GM085267]
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Here we report a facile and efficient method for site directed glycosylation of peptide/protein. The method contains two sequential steps: generation of a GlcNAc-O-peptide/protein, and subsequent ligation of a eukaryotic N-glycan to the GlcNAc moiety. A pharmaceutical peptide, glucagon-like peptide-1 (GLP-1), and a model protein, bovine alpha-Crystallin, were successfully glycosylated using such an approach. It was shown that the GLP-1 with O-linked N-glycan maintained an unchanged secondary structure after glycosylation, suggesting the potential application of this approach for peptide/protein drug production. In summary, the coupled approach provides a general strategy to produce homogeneous glycopeptide/glycoprotein bearing eukaryotic N-glycans.
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