Chemoenzymatic Methods for the Synthesis of Glycoproteins

Glycosylation is one of the most prevalent posttranslational modifications that profoundly affects the structure and functions of proteins in a wide variety of biological recognition events. However, the structural complexity and heterogeneity of glycoproteins, usually resulting from the variations...

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Bibliographic Details
Published in:Chemical reviews 2018-09, Vol.118 (17), p.8359-8413
Main Authors: Li, Chao, Wang, Lai-Xi
Format: Article
Language:English
Subjects:
Catalysis
Chemical synthesis
Chemistry
Enzymes
Glycan
Glycoproteins
Glycoproteins - biosynthesis
Glycoproteins - chemical synthesis
Glycoproteins - chemistry
Glycoside Hydrolases - chemistry
Glycoside Hydrolases - genetics
Glycosylation
Heterogeneity
Organic chemistry
Polypeptides
Polysaccharides - chemistry
Protein Processing, Post-Translational
Proteins
Recombinant Proteins - chemistry
Recombinant Proteins - genetics
Substrate Specificity
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Summary:Glycosylation is one of the most prevalent posttranslational modifications that profoundly affects the structure and functions of proteins in a wide variety of biological recognition events. However, the structural complexity and heterogeneity of glycoproteins, usually resulting from the variations of glycan components and/or the sites of glycosylation, often complicates detailed structure–function relationship studies and hampers the therapeutic applications of glycoproteins. To address these challenges, various chemical and biological strategies have been developed for producing glycan-defined homogeneous glycoproteins. This review highlights recent advances in the development of chemoenzymatic methods for synthesizing homogeneous glycoproteins, including the generation of various glycosynthases for synthetic purposes, endoglycosidase-catalyzed glycoprotein synthesis and glycan remodeling, and direct enzymatic glycosylation of polypeptides and proteins. The scope, limitation, and future directions of each method are discussed.
ISSN:0009-2665
1520-6890
DOI:10.1021/acs.chemrev.8b00238