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Issue 49, 2019
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Traceless synthesis of protein thioesters using enzyme-mediated hydrazinolysis and subsequent self-editing of the cysteinyl prolyl sequence

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Abstract

A traceless thioester-producing protocol featuring carboxypeptidase Y-mediated hydrazinolysis of cysteinyl prolyl leucine-tagged peptides has been developed. The hydrazinolysis followed by thioesterification affords cysteinyl prolyl thioesters. Self-editing of the tag and subsequent trans-thioesterification yields peptide thioesters. The developed protocol was successfully applied to the conversion of recombinant proteins to thioesters.

Graphical abstract: Traceless synthesis of protein thioesters using enzyme-mediated hydrazinolysis and subsequent self-editing of the cysteinyl prolyl sequence

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Publication details

The article was received on 09 May 2019, accepted on 23 May 2019 and first published on 23 May 2019


Article type: Communication
DOI: 10.1039/C9CC03583D
Chem. Commun., 2019,55, 7029-7032

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    Traceless synthesis of protein thioesters using enzyme-mediated hydrazinolysis and subsequent self-editing of the cysteinyl prolyl sequence

    C. Komiya, A. Shigenaga, J. Tsukimoto, M. Ueda, T. Morisaki, T. Inokuma, K. Itoh and A. Otaka, Chem. Commun., 2019, 55, 7029
    DOI: 10.1039/C9CC03583D

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