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

Danilo Hirabae Oliveira, Vasantha Gowda, Tobias Sparrman, Linnea Gustafsson, Rodrigo Sanches Pires, Christian Riekel, Andreas Barth, Christofer Lendel () and My Hedhammar ()
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Danilo Hirabae Oliveira: AlbaNova University Center
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

Nature Communications, 2024, vol. 15, issue 1, 1-14

Abstract: 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.

Date: 2024
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DOI: 10.1038/s41467-024-49111-5

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