Modifications to the enzymatic glycosylation of vancomycin and its residue 4 thioamide analogue are detailed that significantly reduce the enzyme loading and amount of glycosyl donor needed for each glycosylation reaction, provide a streamlined synthesis and replacement for the synthetic UDP-vancosamine glycosyl donor to improve both access and storage stability, and permit a single-pot, two-step conversion of the aglycons to the fully glycosylated synthetic glycopeptides now conducted at higher concentrations. The improvements are exemplified with the two-step, one-pot glycosylation of [Ψ[C(=S)NH]Tpg⁴]vancomycin aglycon (92%) conducted on a 400 mg scale (2 mg–1 g scales) and vancomycin aglycon itself (5 mg scale, 84%).

详细描述了对万古霉素及其残基 4 硫代酰胺类似物的酶促糖基化的修饰，显着降低了每个糖基化反应所需的酶负载和糖基供体的量，提供了合成 UDP-万古胺糖基供体的简化合成和替代，以改善两种途径和储存稳定性，并允许将苷元单罐、两步转化为现在在更高浓度下进行的完全糖基化的合成糖肽。这些改进通过在 400 mg 规模（2 mg–1 g 规模）和万古霉素上进行的 [Ψ[C(=S)NH]Tpg ⁴ ]万古霉素苷元 (92%) 的两步一锅糖基化来例证苷元本身（5 毫克规模，84%）。