ArticleMethods in molecular biology (Clifton, N.J.)2020
Chemoenzymatic Synthesis of HIV-1 Glycopeptide Antigens.
Article in Methods in molecular biology (Clifton, N.J.), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- LC-MS/MS-PRM Quantification of IgG Glycoforms Using Stable Isotope Labeled IgG1 Fc Glycopeptide Standard.Journal of proteome research · 2023Article
- Recent Chemical and Chemoenzymatic Strategies to Complex-TypeFrontiers in chemistry · 2022Review
- Chemoenzymatic Synthesis and Antibody Binding of HIV-1 V1/V2 Glycopeptide-Bacteriophage QInternational journal of molecular sciences · 2021Article
- A facile chemoenzymatic synthesis of SARS-CoV-2 glycopeptides for probing glycosylation functions.Chemical communications (Cambridge, England) · 2021Article
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3 authors.
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Abstract
Glycosylation is one of the most common posttranslational modifications of proteins and can exert profound effects on the inherent properties and biological functions of a given protein. Structurally well-defined homogeneous glycopeptides are highly demanded for functional studies and biomedical applications. Various chemical and chemoenzymatic methods have been reported so far for synthesizing different N- and O-glycopeptides. Among them, the chemoenzymatic method based on an endoglycosidase-catalyzed ligation of free N-glycans and GlcNAc-tagged peptides is emerging as a highly efficient method for constructing large complex N-glycopeptides. This chemoenzymatic approach consists of two key steps. The first step is to prepare the GlcNAc peptide through automated solid-phase peptide synthesis (SPPS) by incorporating an Asn-linked GlcNAc moiety at a predetermined glycosylation site; and the second step is to transfer an N-glycan from the corresponding N-glycan oxazoline en bloc to the GlcNAc peptide by an endoglycosidase or its efficient glycosynthase mutant. In this chapter, we provide detailed procedures of this chemoenzymatic method by demonstrating the synthesis of two HIV-1 V3 glycopeptide antigens carrying a high-mannose-type and a complex-type N-glycan, respectively. The described procedures should be generally applicable for the synthesis of other biologically important N-glycopeptides.
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