Journal
ACS CHEMICAL BIOLOGY
Volume 7, Issue 1, Pages 110-122Publisher
AMER CHEMICAL SOC
DOI: 10.1021/cb200429n
Keywords
Glycoconjugate; Glycoform; Glycosylation; Glycoengineering; Chemoenzymatic; Transglycosylation; Glycoprotein
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Funding
- National Institutes of Health (NIH) [GM080374, GM096973]
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Protein glycosylation is a common and complex posttranslational modification of proteins, which expands functional diversity while boosting structural heterogeneity. Glycoproteins, the end products of such a modification, are typically produced as mixtures of glycoforms possessing the same polypeptide backbone but differing in the site of glycosylation and/or in the structures of pendant glycans, from which single glycoforms are difficult to isolate. The urgent need for glycan-defined glycoproteins in both detailed structure-function relationship studies and therapeutic applications has stimulated an extensive interest in developing various methods for manipulating protein glycosylation. This review highlights emerging technologies that hold great promise in making a variety of glycan-defined glycoproteins, with a particular emphasis in the following three areas: specific glycoengineering of host biosynthetic pathways, in vitro chemoenzymatic glycosylation remodeling, and chemoselective and site specific glycosylation of proteins.
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