Investigation of the stability of thiosialosides toward hydrolysis by sialidases using NMR spectroscopy.
[formula: see text] 1H NMR spectroscopy has been used to investigate whether the alpha(2-->6)-linked thiosialoside 3 and the alpha(2-->3)-linked thiosialoside 9 are hydrolyzed in the presence of Vibrio cholerae sialidase. Similarly, the hydrolysis of the O-ketosides Neu5Ac-2-O-alpha-(2-->3)-Gal beta Me (4) and the alpha-(2-->6)-sialyllactoside 7, representing natural alpha(2-->3)- and alpha(2-->6)-linked sialosides, respectively, was investigated. The results of the 1H NMR experiments clearly demonstrate that the thiosialosides are not hydrolyzed by Vibrio cholerae sialidase. As expected, the O-sialosides are hydrolyzed to give N-acetyl-alpha-D-neuraminic acid as the first product of substrate cleavage.
Wilson
J C
JC
Department of Medicinal Chemistry, Monash University (Parkville Campus), Parkville, Victoria, Australia.
Kiefel
M J
MJ
Angus
D I
DI
von Itzstein
M
M
D002240:Carbohydrate Sequence; D006868:Hydrolysis; D009682:Magnetic Resonance Spectroscopy; D008968:Molecular Conformation; D008969:Molecular Sequence Data; D009439:Neuraminidase / Q000737:chemistry*; D012794:Sialic Acids / Q000737:chemistry; D014734:Vibrio cholerae / Q000737:chemistry
D012794:Sialic Acids; D009439:Neuraminidase