The discovery of a freezing-induced peptide ligation during the total chemical synthesis of human interferon-ε†,Organic & Biomolecular Chemistry

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The discovery of a freezing-induced peptide ligation during the total chemical synthesis of human interferon-ε†
Organic & Biomolecular Chemistry ( IF 2.9 ) Pub Date : 2018-06-25 00:00:00 , DOI: 10.1039/c8ob01365a
Yin-He Yang ₁ , Bin Di , Da-Song Yang

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A counterintuitive freezing-induced peptide ligation was discovered during the total synthesis of human interferon-ε (hIFN-ε) which blocks HIV infection through unique mechanisms. The successful synthesis of hIFN-ε (187 amino acids) in this research laid the foundation for related anti-AIDS drug development. Moreover, alanine mutation based on sequence alignment to solve the maldistribution of the ligation site and freezing-induced dominant conformation that facilitates peptide ligation are expected to be helpful for the synthesis of macrobiomolecules.

中文翻译：

在人干扰素-ε† 的全化学合成过程中发现冷冻诱导的肽连接

在人类干扰素-ε (hIFN-ε) 的全合成过程中发现了一种违反直觉的冷冻诱导肽连接，它通过独特的机制阻止 HIV 感染。本研究成功合成hIFN-ε（187个氨基酸），为相关抗艾滋病药物研发奠定了基础。此外，基于序列比对的丙氨酸突变解决了连接位点的分布不均和冷冻诱导的促进肽连接的显性构象，有望有助于大生物分子的合成。

更新日期：2018-06-25

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