title: Investigation of the stability of thiosialosides toward hydrolysis by sialidases using NMR spectroscopy.
abstract: [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.
authors.affiliation: Department of Medicinal Chemistry, Monash University (Parkville Campus), Parkville, Victoria, Australia.
authors.forename: J C
authors.initials: JC
authors.lastname: Wilson
authors.forename: M J
authors.initials: MJ
authors.lastname: Kiefel
authors.forename: D I
authors.initials: DI
authors.lastname: Angus
authors.forename: M
authors.initials: M
authors.lastname: von Itzstein
mesh_terms: 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
chemical_list: D012794:Sialic Acids; D009439:Neuraminidase