Journal
ORGANIC & BIOMOLECULAR CHEMISTRY
Volume 7, Issue 19, Pages 3982-3990Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/b909091f
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Funding
- Lund University Research School of Medicinal Sciences
- the Swedish Research Council
- the Swedish Strategic Research Foundation
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A fragment-based development of 3C-triazol-1-yl-O-galactopyranosyl aldoximes led to the discovery of highly selective and high affinity (K-d down to 11 mu M) small monosaccharide based inhibitors of galectin-3. Galectin-7, 8 N-terminal CRD, and 9 N-terminal CRD bound the inhibitors only weakly. The galectin-3 selectivity was hypothesized to stem from interaction of the aldoxime moiety with a site not present in the other galectins.
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