期刊
NATURE COMMUNICATIONS
卷 12, 期 1, 页码 -出版社
NATURE PORTFOLIO
DOI: 10.1038/s41467-021-25127-z
关键词
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资金
- National Key Research AMP
- Development Program of China [2018YFA0507602]
- National Natural Science Foundation of China [22031011, 21621002]
- Key Research Program of Frontier Sciences of CAS [ZDBS-LY-SLH030]
- Strategic Priority Research Program of CAS [XDB20020000]
- Youth Innovation Promotion Association of CAS [2020258]
- Shanghai Municipal Science and Technology Major Project
- Shanghai Committee of Science and Technology [17JC1405300]
C-Glycosyl peptides/proteins, stable mimics of native glycopeptides/proteins with therapeutic potential, have been successfully synthesized using a novel method. This synthesis approach is versatile, accommodating a wide range of coupling partners, including complex oligosaccharides and peptide substrates. The resulting vinyl C-glycosyl amino acids and peptides are amenable to further transformations for elongation of peptide and saccharide chains.
C-Glycosyl peptides/proteins are metabolically stable mimics of the native glycopeptides/proteins of great therapeutic potential, but their chemical synthesis is challenging. Here, the authors report a protocol for the synthesis of vinyl C-glycosyl amino acids and peptides, via a Ni-catalyzed reductive hydroglycosylation reaction of alkyne derivatives of amino acids and peptides with glycosyl bromides. C-Glycosyl peptides/proteins are metabolically stable mimics of the native glycopeptides/proteins bearing O/N-glycosidic linkages, and are thus of great therapeutical potential. Herein, we disclose a protocol for the syntheses of vinyl C-glycosyl amino acids and peptides, employing a nickel-catalyzed reductive hydroglycosylation reaction of alkyne derivatives of amino acids and peptides with common glycosyl bromides. It accommodates a wide scope of the coupling partners, including complex oligosaccharide and peptide substrates. The resultant vinyl C-glycosyl amino acids and peptides, which bear common O/N-protecting groups, are amenable to further transformations, including elongation of the peptide and saccharide chains.
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