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‘Click’‐xylosides as initiators of the biosynthesis of glycosaminoglycans: Comparison of mono‐xylosides with xylobiosides
Author(s) -
ChatronColliet Aurore,
Brusa Charlotte,
BertinJung Isabelle,
Gulberti Sandrine,
Ramalanjaoick,
FournelGigleux Sylvie,
Brézillon Stéphane,
Muzard Murielle,
PlantierRoyon Richard,
Rémond Caroline,
Wegrowski Yanusz
Publication year - 2017
Publication title -
chemical biology and drug design
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.59
H-Index - 77
eISSN - 1747-0285
pISSN - 1747-0277
DOI - 10.1111/cbdd.12865
Subject(s) - chemistry , aglycone , biosynthesis , moiety , glycosaminoglycan , priming (agriculture) , galactosyltransferase , stereochemistry , biochemistry , polymerization , enzyme , glycoside , organic chemistry , biology , botany , germination , polymer
Different mono‐xylosides and their corresponding xylobiosides obtained by a chemo‐enzymatic approach featuring various substituents attached to a triazole ring were probed as priming agents for glycosaminoglycan ( GAG ) biosynthesis in the xylosyltransferase‐deficient pgsA‐745 Chinese hamster ovary cell line. Xylosides containing a hydrophobic aglycone moiety were the most efficient priming agents. Mono‐xylosides induced higher GAG biosynthesis in comparison with their corresponding xylobiosides. The influence of the degree of polymerization of the carbohydrate part on the priming activity was investigated through different experiments. We demonstrated that in case of mono‐xylosides, the cellular uptake as well as the affinity and the catalytic efficiency of β‐1,4‐galactosyltransferase 7 were higher than for xylobiosides. Altogether, these results indicate that hydrophobicity of the aglycone and degree of polymerization of glycone moiety were critical factors for an optimal priming activity for GAG biosynthesis.