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Synthetic Glycopeptides from the E‐Selectin Ligand 1 with Varied Sialyl Lewis x Structure as Cell‐Adhesion Inhibitors of E‐Selectin
Author(s) -
Filser Christian,
Kowalczyk Danuta,
Jones Claire,
Wild Martin K.,
Ipe Ute,
Vestweber Dietmar,
Kunz Horst
Publication year - 2007
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200604442
Subject(s) - glycopeptide , fucose , selectin , sialyl lewis x , chemistry , sialic acid , peptide , ligand (biochemistry) , glycan , e selectin , amino acid , adhesion , cell adhesion , stereochemistry , biochemistry , glycoprotein , cell , receptor , organic chemistry , antibiotics
Cooperation is key : Peptide and saccharide portions cooperate in sialyl Lewis x glycopeptides and their mimetics in the fucose and sialic acid parts (see formula), resulting in up to greater than 100‐fold stronger binding to E‐selectin. The synthesis provided sialyl Lewis x amino acids in a form sufficiently acid‐stable for application in automated solid‐phase syntheses of glycopeptides based on acid‐sensitive linkers.