X-ray crystallographic and high-resolution NMR spectroscopy characterization of 4,6-di- O-acetyl-2,3-dideoxy-α- d- erythro-hex-2-enopyranosyl sulfamide

Single crystal X-ray diffraction and high-resolution 1H and 13C NMR spectral data for 4,6-di- O-acetyl-2,3-dideoxy-α- d- erythro-hex-2-enopyranosyl sulfamide, a selective inhibitor of carbonic anhydrase isozyme IX, are reported. The 0 H 5 was found to be the preferred form for this glycosyl sulfamid...

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Bibliographic Details
Published in:Carbohydrate research 2008-11, Vol.343 (17), p.3005-3008
Main Authors: Colinas, Pedro A., Bravo, Rodolfo D., Echeverría, Gustavo A.
Format: Article
Language:English
Subjects:
0H5 conformation
Amino Sugars - chemistry
Carbonic Anhydrase Inhibitors - chemistry
Crystallography, X-Ray - methods
Magnetic Resonance Spectroscopy - methods
Models, Molecular
Molecular Conformation
N-Glycosyl sulfamide
Single crystal
Sulfonamides - chemistry
X-ray diffraction
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Summary:Single crystal X-ray diffraction and high-resolution 1H and 13C NMR spectral data for 4,6-di- O-acetyl-2,3-dideoxy-α- d- erythro-hex-2-enopyranosyl sulfamide, a selective inhibitor of carbonic anhydrase isozyme IX, are reported. The 0 H 5 was found to be the preferred form for this glycosyl sulfamide, both in the crystal lattice and in solution. Single crystal X-ray diffraction and high-resolution 1H and 13C NMR spectral data for 4,6-di- O-acetyl-2,3-dideoxy-α- d- erythro-hex-2-enopyranosyl sulfamide, a selective inhibitor of carbonic anhydrase isozyme IX, are reported. The 0 H 5 was found to be the preferred form for this glycosyl sulfamide, both in the crystal lattice and in solution.
ISSN:0008-6215
1873-426X
DOI:10.1016/j.carres.2008.08.035