Enzymatic synthesis of a sialyl Lewis X dimer from egg yolk as an inhibitor of E-selectin

✍ Scribed by Chun-Hung Lin; Makoto Shimazaki; Chi-Huey Wong; Mamoru Koketsu; Lekh Raj Juneja; Mujo Kim

• Publisher: Elsevier Science
• Year: 1995
• Tongue: English
• Weight: 385 KB
• Volume: 3
• Category: Article
• ISSN: 0968-0896
• DOI: 10.1016/0968-0896(95)00150-6

✦ Synopsis

A dimeric sialyl Lewis X (SLex) glycopeptide was synthesized enzymatically in three steps from an N-linked oligosaccharide prepared from egg yolk. Treatment of delipidated hen egg yolk with the protease Orientase and neuraminidase gave a dimeric N-acetyllactosamine-containing oligosaccharide linked to asparagine. Addition of sialic acid and fucose catalyzed by alpha-2,3-sialyltransferase and alpha-1,3-fucosyltransferase provided the dimeric SLex, which was shown to be as active as monomeric SLex as an inhibitor of E-selectin with IC50 0.75 mM. The synthetic dimeric SLex of the mucin type (i.e. SLex linked to the 3- and 6-OH groups of Gal) is, however, about five times as active as the monomer. It is suggested that dimeric SLex glycopeptides of the mucin type would be effective ligands for E-selectin.