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Molecular sensitised probe for amino acid recognition within peptide sequences

Author

Listed:
  • Xu Wu

    (Max Planck Institute for Solid State Research
    Beijing Institute of Technology)

  • Bogdana Borca

    (Technische Universität Braunschweig
    National Institute of Materials Physics)

  • Suman Sen

    (Max Planck Institute for Solid State Research)

  • Sebastian Koslowski

    (Max Planck Institute for Solid State Research)

  • Sabine Abb

    (Max Planck Institute for Solid State Research)

  • Daniel Pablo Rosenblatt

    (Max Planck Institute for Solid State Research)

  • Aurelio Gallardo

    (Institute of Physics of the Czech Academy of Science
    Charles University)

  • Jesús I. Mendieta-Moreno

    (Institute of Physics of the Czech Academy of Science)

  • Matyas Nachtigall

    (Institute of Physics of the Czech Academy of Science)

  • Pavel Jelinek

    (Institute of Physics of the Czech Academy of Science)

  • Stephan Rauschenbach

    (Max Planck Institute for Solid State Research
    University of Oxford)

  • Klaus Kern

    (Max Planck Institute for Solid State Research
    École Polytechnique Fédérale de Lausanne)

  • Uta Schlickum

    (Max Planck Institute for Solid State Research
    Technische Universität Braunschweig)

Abstract

The combination of low-temperature scanning tunnelling microscopy with a mass-selective electro-spray ion-beam deposition established the investigation of large biomolecules at nanometer and sub-nanometer scale. Due to complex architecture and conformational freedom, however, the chemical identification of building blocks of these biopolymers often relies on the presence of markers, extensive simulations, or is not possible at all. Here, we present a molecular probe-sensitisation approach addressing the identification of a specific amino acid within different peptides. A selective intermolecular interaction between the sensitiser attached at the tip-apex and the target amino acid on the surface induces an enhanced tunnelling conductance of one specific spectral feature, which can be mapped in spectroscopic imaging. Density functional theory calculations suggest a mechanism that relies on conformational changes of the sensitiser that are accompanied by local charge redistributions in the tunnelling junction, which, in turn, lower the tunnelling barrier at that specific part of the peptide.

Suggested Citation

  • Xu Wu & Bogdana Borca & Suman Sen & Sebastian Koslowski & Sabine Abb & Daniel Pablo Rosenblatt & Aurelio Gallardo & Jesús I. Mendieta-Moreno & Matyas Nachtigall & Pavel Jelinek & Stephan Rauschenbach , 2023. "Molecular sensitised probe for amino acid recognition within peptide sequences," Nature Communications, Nature, vol. 14(1), pages 1-8, December.
  • Handle: RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-43844-5
    DOI: 10.1038/s41467-023-43844-5
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    References listed on IDEAS

    as
    1. Sabine Abb & Ludger Harnau & Rico Gutzler & Stephan Rauschenbach & Klaus Kern, 2016. "Two-dimensional honeycomb network through sequence-controlled self-assembly of oligopeptides," Nature Communications, Nature, vol. 7(1), pages 1-7, April.
    2. X. Wu & M. Delbianco & K. Anggara & T. Michnowicz & A. Pardo-Vargas & P. Bharate & S. Sen & M. Pristl & S. Rauschenbach & U. Schlickum & S. Abb & P. H. Seeberger & K. Kern, 2020. "Imaging single glycans," Nature, Nature, vol. 582(7812), pages 375-378, June.
    3. X. Wu & M. Delbianco & K. Anggara & T. Michnowicz & A. Pardo-Vargas & P. Bharate & S. Sen & M. Pristl & S. Rauschenbach & U. Schlickum & S. Abb & P. H. Seeberger & K. Kern, 2020. "Publisher Correction: Imaging single glycans," Nature, Nature, vol. 583(7818), pages 32-32, July.
    4. J. Wade Harper & Eric J. Bennett, 2016. "Proteome complexity and the forces that drive proteome imbalance," Nature, Nature, vol. 537(7620), pages 328-338, September.
    5. Jagannath Swaminathan & Alexander A Boulgakov & Edward M Marcotte, 2015. "A Theoretical Justification for Single Molecule Peptide Sequencing," PLOS Computational Biology, Public Library of Science, vol. 11(2), pages 1-17, February.
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