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Site-Directed Glycosylation of Peptide/Protein with Homogeneous O-Linked Eukaryotic N-Glycans.

ABSTRACT: 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 ?-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.

SUBMITTER: Wu Z

PROVIDER: S-EPMC5951161 | biostudies-literature | 2016 Sep

REPOSITORIES: biostudies-literature

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Site-Directed Glycosylation of Peptide/Protein with Homogeneous O-Linked Eukaryotic N-Glycans.

Wu Zhigang Z Jiang Kuan K Zhu Hailiang H Ma Cheng C Yu Zaikuan Z Li Lei L Guan Wanyi W Liu Yunpeng Y Zhu He H Chen Yanyi Y Li Shanshan S Li Jing J Cheng Jiansong J Zhang Lianwen L Wang Peng George PG

Bioconjugate chemistry 20160818 9

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 α-Crystallin, were successfully glycosylated using such an approach. It was shown that the GLP-1 with O-linked N-glycan maintained an unchanged secondary structu ...[more]

PMID: 27529638

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A combined method for producing homogeneous glycoproteins with eukaryotic N-glycosylation.

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Perturbing the folding energy landscape of the bacterial immunity protein Im7 by site-specific N-linked glycosylation.

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| S-EPMC3012502 | biostudies-literature

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