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A Synthetic Lectin for O‐Linked β‐ N ‐Acetylglucosamine
Author(s) -
Ferrand Yann,
Klein Emmanuel,
Barwell Nicholas P.,
Crump Matthew P.,
JiménezBarbero Jesus,
Vicent Cristina,
Boons GeertJan,
Ingale Sampat,
Davis Anthony P.
Publication year - 2009
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.200804905
Subject(s) - wheat germ agglutinin , lectin , chemistry , glycopeptide , n acetylglucosamine , biochemistry , affinities , galectin , serine , receptor , c type lectin , glycosylation , stereochemistry , agglutinin , phosphorylation , enzyme , antibiotics
Abstract Changing employment : Receptor 1 binds β‐ N ‐acetylglucosaminyl (β‐GlcNAc) up to 100 times more strongly than it does glucose. This synthetic lectin shows affinities similar to wheat germ agglutinin (WGA), a natural lectin used to bind GlcNAc. Remarkably, 1 is more selective than WGA. It favors especially the glycoside unit in glycopeptide 2 , a model of the serine‐ O ‐GlcNAc posttranslational protein modification.