Protein subtype-targeting through ligand epimerization: talose-selectivity of galectin-4 and galectin-8.

Summary, in English

A series of O2 and O3-derivatized methyl beta-d-talopyranosides were synthesized and evaluated in vitro as inhibitors of the galactose-binding galectin-1, -2, -3, -4 (N- and C-terminal domains), 8 (N-terminal domain), and 9 (N-terminal domain). Galectin-4C and 8N were found to prefer the d-talopyranose configuration to the natural ligand d-galactopyranose configuration. Derivatization at talose O2 and/or O3 provided selective submillimolar inhibitors for these two galectins.

• Author: Christopher Öberg; Helen Blanchard; Hakon Leffler; Ulf Nilsson
• Department/s: Centre for Analysis and Synthesis; Division of Microbiology, Immunology and Glycobiology - MIG
• Publishing year: 2008
• Language: English
• Pages: 3691-3694
• Publication/Series: Bioorganic & Medicinal Chemistry Letters
• Volume: 18
• Issue: 13
• Links: http://www.ncbi.nlm.nih.gov/pubmed/18539029?dopt=Abstract; http://dx.doi.org/10.1016/j.bmcl.2008.05.066
• Document type: Journal article
• Publisher: Elsevier
• Topic: Microbiology in the medical area; Immunology in the medical area
• Status: Published
• ISBN/ISSN/Other: ISSN: 0960-894X