Issue 33, 2013
From the journal:

Organic & Biomolecular Chemistry

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

Jerk Rönnols,a   Sophie Manner,b   Anna Siegbahn,b   Ulf Ellervikb  and  Göran Widmalm*a  

* Corresponding authors

a Department of Organic Chemistry, Arrhenius Laboratory, Stockholm University, SE-106 91 Stockholm, Sweden
E-mail: gw@organ.su.se

b Center for Analysis and Synthesis, Chemical Center, Lund University, PO Box 124, SE-221 00 Lund, Sweden

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 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.

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

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Article information

DOI
https://doi.org/10.1039/C3OB40991K
Article type
Paper
Submitted
10 May 2013
Accepted
26 Jun 2013
First published
26 Jun 2013
This article is Open Access
Creative Commons BY license

Org. Biomol. Chem., 2013,11, 5465-5472

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

J. Rönnols, S. Manner, A. Siegbahn, U. Ellervik and G. Widmalm, Org. Biomol. Chem., 2013, 11, 5465 DOI: 10.1039/C3OB40991K

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