Fragment-based development of triazole-substituted O-galactosyl aldoximes with fragment-induced affinity and selectivity for galectin-3.

Summary, in English

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 microm) 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.

• Författare: Johan Tejler; Bader Salameh; Hakon Leffler; Ulf Nilsson
• Avdelning/ar: Centrum för analys och syntes; Avdelningen för mikrobiologi, immunologi och glykobiologi - MIG
• Publiceringsår: 2009
• Språk: Engelska
• Sidor: 3982-3990
• Publikation/Tidskrift/Serie: Organic and Biomolecular Chemistry
• Volym: 7
• Issue: 19
• Länkar: http://dx.doi.org/10.1039/b909091f
• Dokumenttyp: Artikel i tidskrift
• Förlag: Royal Society of Chemistry
• Ämne: Immunology in the medical area; Microbiology in the medical area
• Status: Published
• ISBN/ISSN/Övrigt: ISSN: 1477-0539