Nanofilament organization in highly tough fibers based on lamin proteins.

The escalating plastic pollution crisis necessitates sustainable alternatives, and one promising solution involves replacing petroleum-based polymers with fibrous proteins. This study focused on the recombinant production of intracellular fibrous proteins, specifically Caenorhabditis elegans lamin (Ce-lamin). Ce-lamins spontaneously organize within the cell nucleus, forming a network of nanofilaments. This intricate structure serves as an active layer that responds dynamically to mechanical strain and stress. Herein, we investigated the arrangement of nanofilaments into nanofibrils within wet-spun Ce-lamin fibers using alcoholic solutions as coagulants. Our goal was to understand their structural and mechanical properties, particularly in comparison with those produced with solutions containing Ca+2 ions, which typically result in the formation of nanofibrils with a collagen-like pattern. The introduction of ethanol solutions significantly altered this pattern, likely through rearrangement of the nanofilaments. Nevertheless, the resulting fibers exhibited superior toughness and strain, outperforming various synthetic fibers. The significance of the nanofilament structure in enhancing fiber toughness was emphasized through both the secondary structure transition during stretching and the influence of the Q159K point mutation. This study improves our understanding of the structural and mechanical aspects of Ce-lamin fibers, paving the way for the development of eco-friendly and high-quality fibers suitable for various applications, including medical implants and composite materials.