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Making ends meet: chemically mediated circularization of recombinant proteins.

Cowper, B; Craik, DJ; Macmillan, D; (2013) Making ends meet: chemically mediated circularization of recombinant proteins. Chembiochem , 14 (7) 809 - 812. 10.1002/cbic.201300105. Green open access

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Abstract

A selective N→S 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.

Type: Article
Title: Making ends meet: chemically mediated circularization of recombinant proteins.
Location: Germany
Open access status: An open access version is available from UCL Discovery
DOI: 10.1002/cbic.201300105
Publisher version: http://dx.doi.org/10.1002/cbic.201300105
Language: English
Additional information: � 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. PMCID: PMC4016753
Keywords: Cyclization, Cyclotides, Recombinant Proteins
UCL classification: UCL
UCL > Provost and Vice Provost Offices > UCL BEAMS
UCL > Provost and Vice Provost Offices > UCL BEAMS > Faculty of Maths and Physical Sciences
UCL > Provost and Vice Provost Offices > UCL BEAMS > Faculty of Maths and Physical Sciences > Dept of Chemistry
URI: https://discovery.ucl.ac.uk/id/eprint/1389745
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