Issue 28, 2018

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

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

Supplementary files

Article information

Article type
Communication
Submitted
10 Jun 2018
Accepted
25 Jun 2018
First published
25 Jun 2018

Org. Biomol. Chem., 2018,16, 5097-5101

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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