Probing the carbohydrate recognition domain of E-selectin: the importance of the acid orientation in sLex mimetics

Bioorg Med Chem. 2010 Jan 1;18(1):19-27. doi: 10.1016/j.bmc.2009.11.024. Epub 2009 Nov 13.

Abstract

The selectin-leukocyte interaction is the initial event in the early inflammatory cascade. This interplay proceeds via the terminal tetrasaccharide sialyl Lewis(x) (sLe(x)), present on physiological selectin ligands and E- and P-selectins located on the endothelial surface. Blocking this process is regarded as a promising therapeutic approach for inflammatory diseases where excessive leukocyte efflux is responsible for tissue damage. Selectin antagonists are generally based on sLe(x) as lead structure, containing the essential pharmacophores pre-oriented in the bioactive conformation. In this work, we describe a set of competitive sLe(x) mimetics possessing the carboxylic acid pharmacophore equipped with additional hydrophobic substituents as neuraminic acid (Neu5Ac) replacements. This small library of antagonists derived from Huisgen-1,3-dipolar cycloadditions allows to further probe the carbohydrate recognition domain of E-selectin.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Binding Sites
  • Biomimetics
  • E-Selectin / chemistry*
  • E-Selectin / metabolism*
  • Humans
  • Ligands
  • Models, Molecular
  • Oligosaccharides / chemistry*
  • Oligosaccharides / metabolism
  • Protein Binding
  • Serine / analogs & derivatives*
  • Serine / chemistry
  • Serine / pharmacology
  • Sialyl Lewis X Antigen

Substances

  • E-Selectin
  • Ligands
  • Oligosaccharides
  • Sialyl Lewis X Antigen
  • Serine
  • isoserine