Synthesis of an N-linked glycopeptide from vitamin K-dependent protein S
Synthesis of an N-linked glycopeptide from vitamin K-dependent protein S
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DOI：
10.1016/s0040-4020(98)83053-6
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发表时间：
1998-09-24
期刊：
影响因子：
2.1
通讯作者：
Kihlberg, J
中科院分区：
文献类型：
--
作者：
Holm, B;Linse, S;Kihlberg, J
已经制备了一种新型天冬酰胺结构单元，其具有用酸不稳定TBDMS基团保护的N-连接壳二糖部分。该结构单元用于Fmoc固相合成对应于蛋白S的残基447-460的糖肽片段，其在Asn（458）处具有潜在的N-糖基化位点。壳二糖部分的TBDMS基团在从固相切割糖肽期间被去除，因此与当使用乙酰基保护碳水化合物时相比简化了合成。蛋白S是抗凝血剂，其可以通过C4 b结合蛋白（C4 BP）的络合而失活。发现蛋白S 447-460糖肽是比非糖基化的母体肽更有效的复合物形成抑制剂，表明蛋白S可能在Asn（458）处携带N-连接聚糖。(C)1998 Elsevier Science Ltd.保留所有权利。
A novel asparagine building block having an N-linked chitobiose moiety protected with acid-labile TBDMS groups has been prepared. The building block was used in Fmoc solid-phase synthesis of a glycopeptide fragment corresponding to residues 447-460 of protein S which has a potential N-glycosylation site at Asn(458). The TBDMS groups of the chitobiose moiety were removed during cleavage of the glycopeptide from the solid phase, thus simplifying synthesis as compared to when using acetyl protection for the carbohydrate, Protein S is an anticoagulant which may be inactivated by complexation by C4b binding protein (C4BP). The protein S 447-460 glycopeptide was found to be a more efficient inhibitor of complex formation than the non-glycosylated parent peptide, indicating that protein S may carry an N-linked glycan at Asn(458). (C) 1998 Elsevier Science Ltd. AII rights reserved.