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Chem Biol. 2014 Jan 16;21(1):51-66. doi: 10.1016/j.chembiol.2014.01.001.

Chemical and chemoenzymatic synthesis of glycoproteins for deciphering functions.

Author information

1
Institute of Human Virology and Department of Biochemistry and Molecular Biology, University of Maryland School of Medicine, Baltimore, MD 21201, USA. Electronic address: lwang@som.umaryland.edu.
2
Institute of Human Virology and Department of Biochemistry and Molecular Biology, University of Maryland School of Medicine, Baltimore, MD 21201, USA.

Abstract

Glycoproteins are an important class of biomolecules involved in a number of biological recognition processes. However, natural and recombinant glycoproteins are usually produced as mixtures of glycoforms that differ in the structures of the pendent glycans, which are difficult to separate in pure glycoforms. As a result, synthetic homogeneous glycopeptides and glycoproteins have become indispensable probes for detailed structural and functional studies. A number of elegant chemical and biological strategies have been developed for synthetic construction of tailor-made, full-size glycoproteins to address specific biological problems. In this review, we highlight recent advances in chemical and chemoenzymatic synthesis of homogeneous glycoproteins. Selected examples are given to demonstrate the applications of tailor-made, glycan-defined glycoproteins for deciphering glycosylation functions.

PMID:
24439206
PMCID:
PMC3923302
DOI:
10.1016/j.chembiol.2014.01.001
[Indexed for MEDLINE]
Free PMC Article

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