A Synthetic Lectin for O‐Linked β‐ N ‐Acetylglucosamine | Zendy

Ferrand Yann | Zendy; Klein Emmanuel | Zendy; Barwell Nicholas P. | Zendy; Crump Matthew P. | Zendy; JiménezBarbero Jesus | Zendy; Vicent Cristina | Zendy; Boons GeertJan | Zendy; Ingale Sampat | Zendy; Davis Anthony P. | Zendy

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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

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.

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