Cyclic peptide production using a macrocyclase with enhanced substrate promiscuity and relaxed recognition determinants

Cristina N Alexandru-Crivac, Christian Umeobika, Niina Leikoski, Jouni Jokela, Kirstie Rickaby, Andre M Grilo, Peter Sjo, Alleyn T Plowright, Mohannad Idress, Eike Siebs, Ada Nneoyi-Egbe, Matti Wahlsten, Kaarina Sivonen, Marcel Jaspars, Laurent Trembleau, David P Fewer, Wael E Houssen Ibrahim

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Abstract

Macrocyclic peptides have promising therapeutic potential but the scaling up of their chemical synthesis is challenging. The cyanobactin macrocyclase PatGmac is an efficient tool for production but is limited to substrates containing 6–11 amino acids and at least one thiazoline or proline. Here we report a new cyanobactin macrocyclase that can cyclize longer peptide substrates and those not containing proline/thiazoline and thus allows exploring a wider chemical diversity.
Original languageEnglish
Pages (from-to)10656-10659
Number of pages4
JournalChemical Communications
Volume53
Issue number77
Early online date11 Sep 2017
DOIs
Publication statusPublished - 4 Oct 2017

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  • Cite this

    Alexandru-Crivac, C. N., Umeobika, C., Leikoski, N., Jokela, J., Rickaby, K., Grilo, A. M., Sjo, P., Plowright, A. T., Idress, M., Siebs, E., Nneoyi-Egbe, A., Wahlsten, M., Sivonen, K., Jaspars, M., Trembleau, L., Fewer, D. P., & Houssen Ibrahim, W. E. (2017). Cyclic peptide production using a macrocyclase with enhanced substrate promiscuity and relaxed recognition determinants. Chemical Communications, 53(77), 10656-10659. https://doi.org/10.1039/C7CC05913B