Department of Applied Biochemistry, Institute of Glycoscience, Tokai University, 1117 Kitakaname, Hiratsuka, Kanagawa 259-1292, Japan.
Org Biomol Chem. 2010 Apr 21;8(8):1966-72. doi: 10.1039/b927270d.
The thioester method is a peptide condensation reaction, which requires the protection of Lys side chains for chemoselective ligation. We recently found that the azido group could be used as an amino protecting group in the peptide condensation by the thioester method. In this study, we synthesized the glycosylated mouse pro-opiomelanocortin (1-74) by the thioester method. The N-terminal peptide thioester segment, whose Lys side chain was protected by an azido group, was prepared using a 9-fluorenylmethoxycarbonyl (Fmoc) strategy and an N-alkylcysteine (NAC)-assisted thioesterification reaction. The C-terminal azido-glycopeptide segment carrying N- and O-linked glycans was also prepared by the Fmoc chemistry and condensed with the N-terminal segment by the silver ion-free thioester method. These results showed that our azido-based strategy was fully compatible with the NAC-assisted method and glycoprotein synthesis.
硫酯法是一种肽缩合反应，需要保护赖氨酸侧链以实现化学选择性连接。我们最近发现，叠氮基团可以在硫酯法的肽缩合中用作氨基保护基团。在这项研究中，我们通过硫酯法合成了糖基化的小鼠前阿黑皮素原（1-74）。使用 9-芴甲氧羰基（Fmoc）策略和 N-烷基半胱氨酸（NAC）辅助硫酯化反应制备了 N 端肽硫酯段，其赖氨酸侧链被叠氮基团保护。还通过 Fmoc 化学制备了带有 N 和 O 连接聚糖的 C 端叠氮糖肽段，并通过无银离子硫酯法将其与 N 端段缩合。这些结果表明，我们的基于叠氮的策略与 NAC 辅助方法和糖蛋白合成完全兼容。
