Glycosidase inhibition by ring-modified castanospermine analogues: tackling enzyme selectivity by inhibitor tailoring
Glycosidase inhibition by ring-modified castanospermine analogues: tackling enzyme selectivity by inhibitor tailoring
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DOI：
10.1039/b906968b
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发表时间：
2009-01-01
影响因子：
3.2
通讯作者：
Garcia Fernandez, Jose M.
中科院分区：
文献类型：
--
作者：
Aguilar-Moncayo, Matilde;Gloster, Tracey M.;Garcia Fernandez, Jose M.
合成一组异（硫代）脲型环修饰的栗精胺类似物，其具有自由变旋假异头羟基，导致具有不寻常结合特征的紧密结合的β-葡糖苷酶抑制剂; N-辛基取代基的存在赋予显着的异头选择性，促进β-葡糖苷酶与适当的β-异头物的强结合。
Synthesis of a panel of iso(thio)urea-type ring-modified castanospermine analogues bearing a freely mutarotating pseudoanomeric hydroxyl group results in tight-binding beta-glucosidase inhibitors with unusual binding signatures; the presence of an N-octyl substituent imparts a remarkable anomeric selectivity, promoting strong binding of the appropriate beta-anomer by the beta-glucosidase.