Glycomethanethiosulfonates: powerful reagents for protein glycosylation
Glycomethanethiosulfonates: powerful reagents for protein glycosylation
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DOI：
10.1016/s0957-4166(99)00497-8
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发表时间：
2000-01-28
影响因子：
--
通讯作者：
Jones, JB
中科院分区：
文献类型：
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作者：
Davis, BG;Maughan, MAT;Jones, JB
合成了12种新型糖基硫代磺酸盐（glycomethanethiosulfonate，glyco-MTS）蛋白质糖基化试剂。它们在将定点诱变与化学修饰相结合的受控位点选择性糖基化策略中的使用允许蛋白质糖基化，同时控制（i）位点、（ii）碳水化合物、（iii）异头立体化学、（iv）糖与蛋白质间隔臂的性质和（v）聚糖保护程度。这些高选择性和反应性试剂的能力已经通过使用相应的葡糖-MTS 1和N-Ac-葡糖胺-MTS 2将D-葡糖基和N-Ac-D-葡糖胺基残基引入模型蛋白-丝氨酸蛋白酶枯草杆菌蛋白酶迟缓芽孢杆菌（SBL）中的外部和受阻内部位点来说明。分子模拟研究提供了一个理由，这些试剂对蛋白质的性质显着不同的影响，尽管不同的只是在其C-2取代基的性质。(C)2000爱思唯尔科技有限公司版权所有。
Twelve novel glycomethanethiosulfonate (glyco-MTS) protein glycosylation reagents have been prepared. Their use in a controlled site-selective glycosylation strategy that combines site-directed mutagenesis with chemical modification allows protein glycosylation with concomitant control of (i) site, (ii) carbohydrate, (iii) anomeric stereochemistry, (iv) sugar to protein spacer arm nature and (v) degree of glycan protection. The ability of these highly selective and yet reactive reagents has been illustrated by the introduction of D-glucosyl and N-Ac-D-glucosaminyl residues to both external and hindered internal sites in a model protein - the serine protease enzyme subtilisin Bacillus lentus (SBL) - using corresponding gluco-MTS 1 and N-Ac-glucosamine-MTS 2. Molecular modelling studies provide a rationale for the strikingly different effects of these reagents on the properties of the protein despite differing only in the nature of their C-2 substituents. (C) 2000 Elsevier Science Ltd. All rights reserved.