Abstract
A highly efficient chemoenzymatic synthesis of N-glycopeptides was achieved. It was found that using synthetic oligosaccharide oxazolines, the mimics of the presumed oxazolinium ion intermediate formed in a retaining mechanism of substrate-assisted catalysis, as the donor substrates and GlcNAc-peptides as the acceptors, the endo-beta-N-acetylglucosaminidase (ENGase)-catalyzed transglycosylation gave a high yield (73-82%) of the corresponding glycopeptides in a regio- and stereospecific manner, regardless of the size of the peptide portions. The use of the oligosaccharide oxazolines as donor substrates not only expanded the substrate availability but also led to a substantial enhancement of the synthetic efficiency, compared to the use of natural N-glycans.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Carbohydrate Sequence
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Catalysis
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Glycopeptides / chemistry
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Glycopeptides / metabolism*
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Glycoside Hydrolases / metabolism*
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HIV Envelope Protein gp120 / chemistry
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HIV Envelope Protein gp120 / metabolism
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HIV Envelope Protein gp41 / chemistry
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HIV Envelope Protein gp41 / metabolism
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HIV-1 / chemistry
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HIV-1 / metabolism
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Molecular Sequence Data
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Oligosaccharides / chemistry
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Oligosaccharides / metabolism*
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Oxazolone / analogs & derivatives
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Oxazolone / chemistry
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Oxazolone / metabolism
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Peptide Fragments / chemistry
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Peptide Fragments / metabolism
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Substrate Specificity
Substances
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Glycopeptides
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HIV Envelope Protein gp120
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HIV Envelope Protein gp41
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Oligosaccharides
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Peptide Fragments
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trifluoromethyloxazolinone
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Oxazolone
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Glycoside Hydrolases