The development of a facile cysteine-directed S-glycosylation strategy would facilitate the intensive investigation of the effect of glycosylation on protein translational modification. Herein, we introduce glycosyl Bunte salt as an efficient glycosyl donor for site-selective peptide/protein modification. The coupling reaction with cysteine thiols under alkaline buffer conditions proceeded chemoselectively, delivering homogeneous glycoconjugates and inorganic salt as the only byproduct. A series of sugar moieties, including monosaccharides and oligosaccharides, were successfully conjugated to the peptides and protein via the disulfide bond. Furthermore, this protocol was applied to the glycosylation of the glucagon-like peptide 1 (GLP-1) variant, and its glycosylated effect on blood glucose control was also studied.

一种简便的半胱氨酸导向S 的开发-糖基化策略将有助于深入研究糖基化对蛋白质翻译修饰的影响。在此，我们引入了糖基 Bunte 盐作为用于位点选择性肽/蛋白质修饰的有效糖基供体。在碱性缓冲液条件下与半胱氨酸硫醇的偶联反应以化学选择性进行，提供均质的糖缀合物和无机盐作为唯一的副产物。一系列糖部分，包括单糖和寡糖，通过二硫键成功地与肽和蛋白质结合。此外，该协议还应用于胰高血糖素样肽 1 (GLP-1) 变体的糖基化，还研究了其对血糖控制的糖基化作用。