Synthetic Glycosidase Distinguishing Glycan and Glycosidic Linkage in Its Catalytic Hydrolysis.
Synthetic Glycosidase Distinguishing Glycan and Glycosidic Linkage in Its Catalytic Hydrolysis.
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DOI：
10.1021/acscatal.0c04038
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发表时间：
2020-12-04
期刊：
影响因子：
12.9
通讯作者：
Zhao Y
中科院分区：
文献类型：
--
作者：
Li X;Zhao Y
碳水化合物的选择性水解在生物中对这些分子的加工是至关重要的，但很少用合成催化剂来实现。这一挑战尤其困难，因为催化剂需要区分单个羟基的转化和加入单糖构建块的α或β糖苷键。在这里，我们报道了通过分子印迹在交联胶束中制备的合成糖苷酶。纳米粒子催化剂在尺寸、水溶性和亲水/疏水表面-核心拓扑结构上与天然酶相似。它的硼酸功能化活性中心同时结合了它的目标糖苷底物和一个酸性辅因子，酸性基团靠近外环糖苷氧。疏水锚定的酸性辅因子在酸性中是可调节的，并在中等酸性的水中导致目标糖苷的选择性裂解。通过分子印迹过程，可以合理地设计糖链和α/β糖苷键的选择性。
Selective hydrolysis of carbohydrates is vital to the processing of these molecules in biology but has rarely been achieved with synthetic catalysts. The challenge is especially difficult because the catalyst needs to distinguish the inversion of a single hydroxyl and the α or β glycosidic bonds that join monosaccharide building blocks. Here we report synthetic glycosidase prepared through molecular imprinting within a cross-linked micelle. The nanoparticle catalyst resembles natural enzymes in dimension, water-solubility, and a hydrophilic/hydrophobic surface–core topology. Its boronic acid-functionalized active site binds its targeted glycoside substrate and an acid cofactor simultaneously, with the acidic group in close proximity to the exocyclic glycosidic oxygen. The hydrophobically anchored acid cofactor is tunable in acidity and causes selective cleavage of the targeted glycoside in mildly acidic water. Selectivity for both the glycan and the α/β glycosidic bond can be rationally designed through the molecular imprinting process.
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