Making Ends Meet: Chemically Mediated Circularization of Recombinant Proteins
Article first published online: 4 APR 2013
© 2013 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA. This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
Volume 14, Issue 7, pages 809–812, May 10, 2013
How to Cite
Cowper, B., Craik, D. J. and Macmillan, D. (2013), Making Ends Meet: Chemically Mediated Circularization of Recombinant Proteins. ChemBioChem, 14: 809–812. doi: 10.1002/cbic.201300105
- Issue published online: 29 APR 2013
- Article first published online: 4 APR 2013
- Manuscript Received: 26 FEB 2013
- Funded Access
- UK Engineering and Physical Sciences Research Council. Grant Number: EP/J007560/1
- acyl transfer;
- native chemical ligation;
- protein engineering
A selective NS acyl transfer reaction facilitates semi-synthesis of the plant cyclotide kalata B1 from a linear precursor peptide of bacterial origin, through simple appendage of N-terminal cysteine and a thiol-labile C-terminal Gly-Cys motif. This constitutes the first synthesis of a ribosomally derived circular miniprotein, without recourse to protein splicing elements.