Synthetic Glycopeptides from the E‐Selectin Ligand 1 with Varied Sialyl Lewis x  Structure as Cell‐Adhesion Inhibitors of E‐Selectin | Zendy

Filser Christian | Zendy; Kowalczyk Danuta | Zendy; Jones Claire | Zendy; Wild Martin K. | Zendy; Ipe Ute | Zendy; Vestweber Dietmar | Zendy; Kunz Horst | Zendy

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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.

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