A Synthetic Lectin for O-Linked β-N-Acetylglucosamine

被引：116

作者：

Ferrand, Yann ^{[1
]}

Klein, Emmanuel ^{[1
]}

Barwell, Nicholas P. ^{[1
]}

Crump, Matthew P. ^{[1
]}

Jimenez-Barbero, Jesus ^{[2
]}

Vicent, Cristina ^{[3
]}

Boons, Geert-Jan ^{[4
]}

Ingale, Sampat ^{[4
]}

Davis, Anthony P. ^{[1
]}

机构：

[1] Univ Bristol, Sch Chem, Bristol BS8 1TS, Avon, England

[2] CSIC, Ctr Invest Biol, Madrid, Spain

[3] CSIC, Inst Quim Organ, E-28006 Madrid, Spain

[4] Univ Georgia, Complex Carbohydrate Res Ctr, Athens, GA 30602 USA

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2009年 / 48卷 / 10期

基金：

英国工程与自然科学研究理事会;

关键词：

biomimetic hosts; carbohydrates; molecular recognition; receptors; supramolecular chemistry; WHEAT-GERM-AGGLUTININ; CARBOHYDRATE-BINDING; NUCLEOCYTOPLASMIC PROTEINS; RECOGNITION; GLCNAC; GLYCOSYLATION; SPECIFICITY; RECEPTORS; WATER; GLYCOBIOLOGY;

D O I：

10.1002/anie.200804905

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

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. © 2009 Wiley-VCH Verlag GmbH & Co. KGaA.

引用

页码：1775 / 1779

页数：5

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