Exploration of conformational flexibility and hydrogen bonding of xylosides in different solvents, as a model system for enzyme active site interactions

Org Biomol Chem. 2013 Sep 7;11(33):5465-72. doi: 10.1039/c3ob40991k.

Abstract

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 (4)C1, (2)SO and (1)C4 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 (1h)JF4,HO2 coupling. Hydrogen bond directionality was further established via comparisons of fluorinated levoglucosan molecules.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Catalytic Domain*
  • Glycosides / chemistry*
  • Hydrogen Bonding
  • Magnetic Resonance Spectroscopy
  • Models, Molecular*
  • Molecular Conformation
  • Solvents / chemistry

Substances

  • Glycosides
  • Solvents
  • xylosides