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

  • Bioorg Med Chem Lett. 2008 Jul 1;18(13):3691-4. doi: 10.1016/j.bmcl.2008.05.066.
Christopher T Oberg  1 ,  Helen Blanchard ,  Hakon Leffler ,  Ulf J Nilsson
Affiliations
  • 1. Organic Chemistry, Lund University, PO Box 124, SE-221 00 Lund, Sweden.
PMID: 18539029 DOI: 10.1016/j.bmcl.2008.05.066
Abstract

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.

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