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Chemoenzymatic synthesis of dendritic sialyl Lewisx

Authors
Journal
Carbohydrate Research
0008-6215
Publisher
Elsevier
Publication Date
Volume
305
Identifiers
DOI: 10.1016/s0008-6215(97)00263-2
Keywords
  • Sialyl Lewisx
  • Dendrimers
  • Enzymes
  • L-Lysine
Disciplines
  • Chemistry

Abstract

Abstract Traditional structure activity relationship studies (SAR) have led to the development of numerous sialyl Lewis x analogs in the search for potential antiinflammatory agents. However, these methods do not take into account cluster or multivalent effects. Reported herein is the chemoenzymatic synthesis of di-, tetra-, and octa-valent sLe x ligands scaffolded on dendrimers. Hypervalent l-lysine cores with covalently attached 2-acetamido-2-deoxy- d-glucose ( N-acetylglucosamine, GlcNAc) residues were chemically prepared and enzymatically transformed into sLe x-containing dendrimers so that multivalency, and its role in selectin-sLe x interactions may be evaluated. This work constitutes another successful enzymatic synthesis of sLe x and represents the first example of GlcNAc elongation on a synthetic dendrimer scaffold. These sLe x dendrimers are currently being investigated as selectin antagonists.

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