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Exo-chirality of the α-helix

Author

Listed:
  • Jose M. Martínez-Parra

    (Universidade de Santiago de Compostela)

  • Rebeca Gómez-Ojea

    (Universidade de Santiago de Compostela)

  • Geert A. Daudey

    (Universidade de Santiago de Compostela)

  • Martin Calvelo

    (Universidade de Santiago de Compostela)

  • Hector Fernández-Caro

    (Universidade de Santiago de Compostela)

  • Javier Montenegro

    (Universidade de Santiago de Compostela)

  • Julian Bergueiro

    (Universidade de Santiago de Compostela)

Abstract

The structure of helical polymers is dictated by the molecular chirality of their monomer units. Particularly, macromolecular helices with monomer sequence control have the potential to generate chiral topologies. In α-helical folded peptides, the sequential repetition of amino acids generates a chiral layer defined by the amino acid side chains projected outside the amide backbone. Despite being closely related to peptides’ structural and functional properties, to the best of our knowledge, a general exo-helical symmetry model has not been yet described for the α-helix. Here, we perform the theoretical, computational, and spectroscopic elucidation of the α-helix principal exo-helical topologies. Non-canonical labeled amino acids are employed to spectroscopically characterize the different exo-helical topologies in solution, which precisely match the theorical prediction. Backbone-to-chromophore distance also shows the expected impact in the exo-helices’ geometry and spectroscopic fingerprint. Theoretical prediction and spectroscopic validation of this exo-helical topological model provides robust experimental evidence of the chiral potential on the surface of helical peptides and outlines an entirely new structural scenario for the α-helix.

Suggested Citation

  • Jose M. Martínez-Parra & Rebeca Gómez-Ojea & Geert A. Daudey & Martin Calvelo & Hector Fernández-Caro & Javier Montenegro & Julian Bergueiro, 2024. "Exo-chirality of the α-helix," Nature Communications, Nature, vol. 15(1), pages 1-8, December.
  • Handle: RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-51072-8
    DOI: 10.1038/s41467-024-51072-8
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    References listed on IDEAS

    as
    1. Alan Saghatelian & Yohei Yokobayashi & Kathy Soltani & M. Reza Ghadiri, 2001. "A chiroselective peptide replicator," Nature, Nature, vol. 409(6822), pages 797-801, February.
    2. Po-Ssu Huang & Scott E. Boyken & David Baker, 2016. "The coming of age of de novo protein design," Nature, Nature, vol. 537(7620), pages 320-327, September.
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