Exploration of conformational flexibility and hydrogen bonding of xylosides in different solvents, as a model system for enzyme active site interactions
2013 (English)In: Organic and biomolecular chemistry, ISSN 1477-0520, E-ISSN 1477-0539, Vol. 11, no 33, 5465-5472 p.Article in journal (Refereed) Published
The predominantly populated conformation of carbohydrates in solution does not necessarily represent the biologically active species; rather, any conformer accessible without too large an energy penalty may be present in a biological pathway. Thus, the conformational preferences of a naphthyl xyloside, which initiates in vivo synthesis of antiproliferative glycosaminoglycans, have been studied by using NMR spectroscopy in a variety of solvents. Equilibria comprising the conformations 4C1, 2SO and 1C4 were found, with a strong dependence on the hydrogen bonding ability of the solvent. Studies of fluorinated analogues revealed a direct hydrogen bond from the hydroxyl group at C2 to the fluorine atom at C4 by a 1hJF4,HO2 coupling. Hydrogen bond directionality was further established via comparisons of fluorinated levoglucosan molecules.
Place, publisher, year, edition, pages
2013. Vol. 11, no 33, 5465-5472 p.
Research subject Organic Chemistry
IdentifiersURN: urn:nbn:se:su:diva-92472DOI: 10.1039/C3OB40991KISI: 000323141800010OAI: oai:DiVA.org:su-92472DiVA: diva2:639381
FunderSwedish Research CouncilKnut and Alice Wallenberg Foundation