Ferrand Yann, Klein Emmanuel, Barwell Nicholas P, Crump Matthew P, Jiménez-Barbero Jesus, Vicent Cristina, Boons Geert-Jan, Ingale Sampat, Davis Anthony P
School of Chemistry, University of Bristol, Cantock's Close, Bristol, BS8 1TS, UK.
Angew Chem Int Ed Engl. 2009;48(10):1775-9. doi: 10.1002/anie.200804905.
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.
受体1与β-N-乙酰葡糖胺(β-GlcNAc)的结合强度比其与葡萄糖的结合强度高多达100倍。这种合成凝集素表现出与麦胚凝集素(WGA,一种用于结合GlcNAc的天然凝集素)相似的亲和力。值得注意的是,1比WGA更具选择性。它特别倾向于糖肽2中的糖苷单元,糖肽2是丝氨酸-O-GlcNAc翻译后蛋白质修饰的模型。