作者: Antoine Petrelli , Eric Samain , Stéphanie Pradeau , Sami Halila , Sébastien Fort
关键词:
摘要: Glycan-protein interactions play a crucial role in physiological and pathological events. Hence, improving the isolation of carbohydrate-binding proteins (i.e. lectins anti-glycan antibodies) from complex media can not only lead to better understanding their function, but also provides solutions for public health issues, such as water contamination or need universal blood plasma. Herein, we report rapid efficient method produce carbohydrate-based affinity adsorbents combining enzymatic synthesis metal-free click chemistry. Simple well glycans (maltose, group antigens A, B H) were readily modified by addition furyl at reducing end without protecting groups then efficiently conjugated maleimide-activated Sepharose particles via Diels-Alder reaction. These neoglycoconjugates showed high efficiency purification (Concanavalin A Ulex europaeus agglutinin) capture anti-A anti-B antibodies, opening new prospects glycoproteomics development