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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

Ronnols, Jerk; Manner, Sophie LU ; Siegbahn, Anna LU ; Ellervik, Ulf LU and Widmalm, Goran (2013) In Organic and Biomolecular Chemistry 11(33). p.5465-5472
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 C-4(1), S-2(0) and C-1(4) 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)J(F4,HO2)... (More)
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 C-4(1), S-2(0) and C-1(4) 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)J(F4,HO2) coupling. Hydrogen bond directionality was further established via comparisons of fluorinated levoglucosan molecules. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Organic and Biomolecular Chemistry
volume
11
issue
33
pages
5465 - 5472
publisher
Royal Society of Chemistry
external identifiers
  • wos:000323141800010
  • scopus:84881122050
ISSN
1477-0539
DOI
10.1039/c3ob40991k
language
English
LU publication?
yes
id
94535941-a6f6-4ced-8348-c04526ee8e28 (old id 4025578)
date added to LUP
2013-10-08 12:59:06
date last changed
2019-02-20 01:59:44
@article{94535941-a6f6-4ced-8348-c04526ee8e28,
  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 C-4(1), S-2(0) and C-1(4) 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)J(F4,HO2) coupling. Hydrogen bond directionality was further established via comparisons of fluorinated levoglucosan molecules.},
  author       = {Ronnols, Jerk and Manner, Sophie and Siegbahn, Anna and Ellervik, Ulf and Widmalm, Goran},
  issn         = {1477-0539},
  language     = {eng},
  number       = {33},
  pages        = {5465--5472},
  publisher    = {Royal Society of Chemistry},
  series       = {Organic and Biomolecular Chemistry},
  title        = {Exploration of conformational flexibility and hydrogen bonding of xylosides in different solvents, as a model system for enzyme active site interactions},
  url          = {http://dx.doi.org/10.1039/c3ob40991k},
  volume       = {11},
  year         = {2013},
}