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J Am Chem Soc. 2011 Oct 12;133(40):16127-35. doi: 10.1021/ja206023e. Epub 2011 Sep 14.

Protein glycoengineering enabled by the versatile synthesis of aminooxy glycans and the genetically encoded aldehyde tag.

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1
Department of Chemistry and Howard Hughes Medical Institute, University of California, Berkeley, California 94720, USA.

Abstract

Homogeneously glycosylated proteins are important targets for fundamental research and for biopharmaceutical development. The use of unnatural protein-glycan linkages bearing structural similarity to their native counterparts can accelerate the synthesis of glycoengineered proteins. Here we report an approach toward generating homogeneously glycosylated proteins that involves chemical attachment of aminooxy glycans to recombinantly produced proteins via oxime linkages. We employed the recently introduced aldehyde tag method to obtain a recombinant protein with the aldehyde-bearing formylglycine residue at a specific site. Complex aminooxy glycans were synthesized using a new route that features N-pentenoyl hydroxamates as key intermediates that can be readily elaborated chemically and enzymatically. We demonstrated the method by constructing site-specifically glycosylated variants of the human growth hormone.

PMID:
21866965
PMCID:
PMC3187659
DOI:
10.1021/ja206023e
[Indexed for MEDLINE]
Free PMC Article
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