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  • Title: Probing the carbohydrate recognition domain of E-selectin: the importance of the acid orientation in sLex mimetics.
    Author: Titz A, Patton J, Smiesko M, Radic Z, Schwardt O, Magnani JL, Ernst B.
    Journal: Bioorg Med Chem; 2010 Jan 01; 18(1):19-27. PubMed ID: 19948406.
    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.
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