Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 133, Issue 41, Pages 16495-16502Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ja205392z
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Funding
- Ministerio de Ciencia e Innovacion [CTQ2008-04444/BQA]
- Government of the Basque Country
- Etortek grant
- European Union [PITN-GA-2008-215536]
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Two recombinant fucosyltransferases were employed as synthetic tools in the chemoenzymatic synthesis of core fucosylated N-glycan structures. Enzyme substrates were rapidly identified by incubating a microarray of synthetic N-glycans with the transferases and detecting the presence of core fucose with four lectins and one antibody. Selected substrates were then enzymatically fucosylated in solution on a preparative scale and characterized by NMR and MS. With this approach the chemoenzymatic synthesis of a series of alpha 1,3-, alpha 1,6-, and difucosylated structures was accomplished in very short time and with high yields, which otherwise would have required extensive additional synthetic effort and a complete redesign of existing synthetic routes. In addition, valuable information was gathered regarding the specificities of the lectins employed in this study.
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