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

Guillaume De Bo; Malcolm Gall; Matthew Kitching; Sonja Kuschel; David Leigh; Daniel Tetlow; John Ward

doi:10.1021/jacs.7b05850

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

Guillaume De Bo, Malcolm Gall, Matthew Kitching, Sonja Kuschel, David Leigh, Daniel Tetlow, John Ward

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Abstract

We report on the synthesis and operation of a three-barrier, rotaxane-based, artificial molecular machine capable of sequence-specific beta-homo (β3) peptide synthesis. The machine utilizes non-proteinogenic 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.

Original language	English
Journal	American Chemical Society. Journal
Early online date	19 Jul 2017
DOIs	https://doi.org/10.1021/jacs.7b05850
Publication status	Published - 2017

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10.1021/jacs.7b05850

BetaPepSyn - JACS2017 - AAMAccepted author manuscript, 1.23 MB

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title = "Sequence-Specific Beta-Peptide Synthesis by a Rotaxane- Based Molecular Machine",

abstract = "We report on the synthesis and operation of a three-barrier, rotaxane-based, artificial molecular machine capable of sequence-specific beta-homo (β3) peptide synthesis. The machine utilizes non-proteinogenic 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.",

author = "{De Bo}, Guillaume and Malcolm Gall and Matthew Kitching and Sonja Kuschel and David Leigh and Daniel Tetlow and John Ward",

year = "2017",

doi = "10.1021/jacs.7b05850",

language = "English",

journal = "American Chemical Society. Journal ",

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T1 - Sequence-Specific Beta-Peptide Synthesis by a Rotaxane- Based Molecular Machine

AU - De Bo, Guillaume

AU - Gall, Malcolm

AU - Kitching, Matthew

AU - Kuschel, Sonja

AU - Leigh, David

AU - Tetlow, Daniel

AU - Ward, John

PY - 2017

Y1 - 2017

N2 - We report on the synthesis and operation of a three-barrier, rotaxane-based, artificial molecular machine capable of sequence-specific beta-homo (β3) peptide synthesis. The machine utilizes non-proteinogenic 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.

AB - We report on the synthesis and operation of a three-barrier, rotaxane-based, artificial molecular machine capable of sequence-specific beta-homo (β3) peptide synthesis. The machine utilizes non-proteinogenic 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.

UR - http://dro.dur.ac.uk/22931/

U2 - 10.1021/jacs.7b05850

DO - 10.1021/jacs.7b05850

M3 - Article

SN - 0002-7863

JO - American Chemical Society. Journal

JF - American Chemical Society. Journal

ER -

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

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