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Protecting‐Group‐Controlled Enzymatic Glycosylation of Oligo‐ N ‐Acetyllactosamine Derivatives
Author(s) -
Gagarinov Ivan A.,
Li Tiehai,
Wei Na,
Sastre Toraño Javier,
de Vries Robert P.,
Wolfert Margreet A.,
Boons GeertJan
Publication year - 2019
Publication title -
angewandte chemie
Language(s) - English
Resource type - Journals
eISSN - 1521-3757
pISSN - 0044-8249
DOI - 10.1002/ange.201903140
Subject(s) - fucosylation , chemistry , glycosylation , glycan , biochemistry , glycoconjugate , transferase , fucosyltransferase , enzyme , amine gas treating , protecting group , glycoside hydrolase , stereochemistry , glycoprotein , organic chemistry , alkyl
We describe a chemoenzymatic strategy that can give a library of differentially fucosylated and sialylated oligosaccharides starting from a single chemically synthesized tri‐ N ‐acetyllactosamine derivative. The common precursor could easily be converted into 6 different hexasaccharides in which the glucosamine moieties are either acetylated (GlcNAc) or modified as a free amine (GlcNH 2 ) or Boc (GlcNHBoc). Fucosylation of the resulting compounds by a recombinant fucosyl transferase resulted in only modification of the natural GlcNAc moieties, providing access to 6 selectively mono‐ and bis‐fucosylated oligosaccharides. Conversion of the GlcNH 2 or GlcNHBoc moieties into the natural GlcNAc, followed by sialylation by sialyl transferases gave 12 differently fucosylated and sialylated compounds. The oligosaccharides were printed as a microarray that was probed by several glycan‐binding proteins, demonstrating that complex patterns of fucosylation can modulate glycan recognition.