Enabling N-to-C Ser/Thr Ligation for Convergent Protein Synthesis via Combining Chemical Ligation Approaches,Journal of the American Chemical Society

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Enabling N-to-C Ser/Thr Ligation for Convergent Protein Synthesis via Combining Chemical Ligation Approaches
Journal of the American Chemical Society ( IF 14.4 ) Pub Date : 2016-08-15 , DOI: 10.1021/jacs.6b04238
Chi Lung Lee ₁ , Han Liu ₁ , Clarence T. T. Wong ₁ , Hoi Yee Chow ₁ , Xuechen Li ₁

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In this article, Ser/Thr ligation(on/off) has been realized to enable N-to-C successive peptide ligations using a salicylaldehyde semicarbazone (SAL(off)) group by in situ activation with pyruvic acid of the peptide SAL(off) ester into the peptide salicylaldehyde (SAL(on)) ester. In addition, a peptide with a C-terminal thioester and N-terminal Ser or Thr as the middle peptide segment can undergo one-pot Ser/Thr ligation and native chemical ligation in the N-to-C direction. The utility of this combined ligation strategy in the N-to-C direction has been showcased through the convergent assembly of a human cytokine protein sequence, GlcNAcylated interleukin-25.

中文翻译：

通过结合化学连接方法实现 N-to-C Ser/Thr 连接以进行聚合蛋白质合成

在本文中，Ser/Thr ligation(on/off) 实现了使用水杨醛缩氨基脲 (SAL(off)) 基团通过肽 SAL(off) 的丙酮酸原位激活实现 N 到 C 连续肽连接。 ) 酯转化为肽水杨醛 (SAL(on)) 酯。此外，具有 C 端硫酯和 N 端 Ser 或 Thr 作为中间肽段的肽可以在 N 到 C 方向上进行单锅 Ser/Thr 连接和天然化学连接。这种组合连接策略在 N 到 C 方向的效用已通过人类细胞因子蛋白序列 GlcNAcylated interleukin-25 的会聚组装得到展示。

更新日期：2016-08-15

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