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JOURNAL ARTICLE
RESEARCH SUPPORT, NON-U.S. GOV'T
Fucosyltransferases as synthetic tools: glycan array based substrate selection and core fucosylation of synthetic N-glycans.
Journal of the American Chemical Society 2011 October 20
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 α1,3-, α1,6-, 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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