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Sequence-Specific β-Peptide Synthesis by a Rotaxane-Based Molecular Machine

De Bo, Guillaume; Gall, Malcolm A.Y.; Kitching, Matthew O.; Kuschel, Sonja; Leigh, David A.; Tetlow, Daniel J.; Ward, John W.

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Authors

Guillaume De Bo

Malcolm A.Y. Gall

Sonja Kuschel

David A. Leigh

Daniel J. Tetlow

John W. Ward



Abstract

We report on the synthesis and operation of a three-barrier, rotaxane-based, artificial molecular machine capable of sequence-specific β-homo (β3) peptide synthesis. The machine utilizes nonproteinogenic β3-amino acids, a class of amino acids not generally accepted by the ribosome, particularly consecutively. Successful operation of the machine via native chemical ligation (NCL) demonstrates that even challenging 15- and 19-membered ligation transition states are suitable for information translation using this artificial molecular machine. The peptide-bond-forming catalyst region can be removed from the transcribed peptide by peptidases, artificial and biomachines working in concert to generate a product that cannot be made by either machine alone.

Citation

De Bo, G., Gall, M. A., Kitching, M. O., Kuschel, S., Leigh, D. A., Tetlow, D. J., & Ward, J. W. (2017). Sequence-Specific β-Peptide Synthesis by a Rotaxane-Based Molecular Machine. Journal of the American Chemical Society, 139(31), 10875-10879. https://doi.org/10.1021/jacs.7b05850

Journal Article Type Article
Online Publication Date Jul 26, 2017
Publication Date Aug 9, 2017
Deposit Date Sep 18, 2017
Publicly Available Date Jul 19, 2018
Journal Journal of the American Chemical Society
Print ISSN 0002-7863
Electronic ISSN 1520-5126
Publisher American Chemical Society
Peer Reviewed Peer Reviewed
Volume 139
Issue 31
Pages 10875-10879
DOI https://doi.org/10.1021/jacs.7b05850

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Accepted Journal Article (920 Kb)
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Copyright Statement
This document is the Accepted Manuscript version of a Published Work that appeared in final form in Journal of the American Chemical Society, copyright © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see https://doi.org/10.1021/jacs.7b05850.







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