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A synthetic lectin for O-linked beta-N-acetylglucosamine.


ABSTRACT: Changing employment: Receptor 1 binds beta-N-acetylglucosaminyl (beta-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.

SUBMITTER: Ferrand Y 

PROVIDER: S-EPMC2835298 | biostudies-literature | 2009

REPOSITORIES: biostudies-literature

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A synthetic lectin for O-linked beta-N-acetylglucosamine.

Ferrand Yann Y   Klein Emmanuel E   Barwell Nicholas P NP   Crump Matthew P MP   Jiménez-Barbero Jesus J   Vicent Cristina C   Boons Geert-Jan GJ   Ingale Sampat S   Davis Anthony P AP  

Angewandte Chemie (International ed. in English) 20090101 10


Changing employment: Receptor 1 binds beta-N-acetylglucosaminyl (beta-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. ...[more]

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