In vitro experimental study demonstrates distinct phase separation behavior between recombinant MaSp1 and MaSp2 spidroins, suggesting mechanisms for hierarchical fiber assembly.
Spider silk fibers show exceptional mechanical properties, based on their underlying spider silk proteins (spidroins) as well as a highly developed spinning process, involving the transition of soluble high-molecular-weight spidroins into a hierarchically structured solid fiber. Liquid-liquid-phase separation is crucial for the transition of the liquid to the solid state. Here, the assembly properties of a newly designed recombinant major ampullate spidroin 1 derivative based on an Araneus sequence have been investigated. Interestingly, the protein phase-separates at slightly chaotropic conditions in contrast to respective MaSp2-derived variants from Araneus. Fibers spun from the MaSp1-derivative as well as MaSp1-MaSp2-mixtures provide a deeper insight into the assembly process of the spidroins and how hierarchical architectures of spider silk fibers could be achieved.
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Schiller et al. (2026) studied this question.
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