Site-selective chemoenzymatic construction of synthetic glycoproteins using endoglycosidases
Site-selective chemoenzymatic construction of synthetic glycoproteins using endoglycosidases
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DOI：
10.1039/c0sc00265h
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发表时间：
2010-01-01
期刊：
影响因子：
8.4
通讯作者：
Davis, Benjamin G.
中科院分区：
文献类型：
--
作者：
Fernandez-Gonzalez, Marta;Boutureira, Omar;Davis, Benjamin G.
结合化学标记，然后进行Endo-A催化的延伸，可以获得均匀的、精心制作的糖蛋白。对不同键和糖的调查表明，不仅可以容忍非天然键，而且它们可以提供对Endo-A转糖基化活性范围的洞察。S-连接的GlcNAc-糖蛋白是用于Endo-A延伸的有用底物，并且在暴露位点处显示增强的水解稳定性。O-CH（2）-三唑连接的GlcNAc-糖蛋白衍生自叠氮基高丙氨酸标记的蛋白质前体被发现是最佳的空间要求的网站。
Combined chemical tagging followed by Endo-A catalysed elongation allows access to homogeneous, elaborated glycoproteins. A survey of different linkages and sugars demonstrated not only that unnatural linkages can be tolerated but they can provide insight into the scope of Endo-A transglycosylation activity. S-linked GlcNAc-glycoproteins are useful substrates for Endo-A extensions and display enhanced stability to hydrolysis at exposed sites. O-CH(2)-triazole-linked GlcNAc-glycoproteins derived from azidohomoalanine-tagged protein precursors were found to be optimal at sterically demanding sites.