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Structural conversion of the spidroin C-terminal domain during assembly of spider silk fibers

Author

Listed:
  • Danilo Hirabae Oliveira

    (AlbaNova University Center
    KTH Royal Institute of Technology)

  • Vasantha Gowda

    (KTH Royal Institute of Technology)

  • Tobias Sparrman

    (Umeå University)

  • Linnea Gustafsson

    (Spiber Technologies AB)

  • Rodrigo Sanches Pires

    (KTH Royal Institute of Technology)

  • Christian Riekel

    (European Synchrotron Radiation Facility, B.P. 220)

  • Andreas Barth

    (Stockholm University)

  • Christofer Lendel

    (KTH Royal Institute of Technology)

  • My Hedhammar

    (AlbaNova University Center)

Abstract

The major ampullate Spidroin 1 (MaSp1) is the main protein of the dragline spider silk. The C-terminal (CT) domain of MaSp1 is crucial for the self-assembly into fibers but the details of how it contributes to the fiber formation remain unsolved. Here we exploit the fact that the CT domain can form silk-like fibers by itself to gain knowledge about this transition. Structural investigations of fibers from recombinantly produced CT domain from E. australis MaSp1 reveal an α-helix to β-sheet transition upon fiber formation and highlight the helix No4 segment as most likely to initiate the structural conversion. This prediction is corroborated by the finding that a peptide corresponding to helix No4 has the ability of pH-induced conversion into β-sheets and self-assembly into nanofibrils. Our results provide structural information about the CT domain in fiber form and clues about its role in triggering the structural conversion of spidroins during fiber assembly.

Suggested Citation

  • Danilo Hirabae Oliveira & Vasantha Gowda & Tobias Sparrman & Linnea Gustafsson & Rodrigo Sanches Pires & Christian Riekel & Andreas Barth & Christofer Lendel & My Hedhammar, 2024. "Structural conversion of the spidroin C-terminal domain during assembly of spider silk fibers," Nature Communications, Nature, vol. 15(1), pages 1-14, December.
    • Handle: RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-49111-5
    DOI: 10.1038/s41467-024-49111-5
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    References listed on IDEAS

    as
    1. Glareh Askarieh & My Hedhammar & Kerstin Nordling & Alejandra Saenz & Cristina Casals & Anna Rising & Jan Johansson & Stefan D. Knight, 2010. "Self-assembly of spider silk proteins is controlled by a pH-sensitive relay," Nature, Nature, vol. 465(7295), pages 236-238, May.
    2. Franz Hagn & Lukas Eisoldt & John G. Hardy & Charlotte Vendrely & Murray Coles & Thomas Scheibel & Horst Kessler, 2010. "A conserved spider silk domain acts as a molecular switch that controls fibre assembly," Nature, Nature, vol. 465(7295), pages 239-242, May.
    3. Charlotte Rat & Julia C. Heiby & Jessica P. Bunz & Hannes Neuweiler, 2018. "Two-step self-assembly of a spider silk molecular clamp," Nature Communications, Nature, vol. 9(1), pages 1-11, December.
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