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Issue 28, 2018
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The discovery of a freezing-induced peptide ligation during the total chemical synthesis of human interferon-ε

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Abstract

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.

Graphical abstract: The discovery of a freezing-induced peptide ligation during the total chemical synthesis of human interferon-ε

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Publication details

The article was received on 10 Jun 2018, accepted on 25 Jun 2018 and first published on 25 Jun 2018


Article type: Communication
DOI: 10.1039/C8OB01365A
Citation: Org. Biomol. Chem., 2018,16, 5097-5101
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    The discovery of a freezing-induced peptide ligation during the total chemical synthesis of human interferon-ε

    Y. Yang, B. Di and D. Yang, Org. Biomol. Chem., 2018, 16, 5097
    DOI: 10.1039/C8OB01365A

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