Silk has attracted widespread attention due to its superlative material properties and promising applications. However, the determinants behind the variations in material properties among different types of silk are not well understood. We analysed the physical properties of silk samples from a variety of silkmoth cocoons, including domesticated Bombyx mori varieties and several species from Saturniidae. Tensile deformation tests, thermal analyses, and investigations on crystalline structure and orientation of the fibres were performed. The results showed that saturniid silks produce more highly-defined structural transitions compared to B. mori, as seen in the yielding and strain hardening events during tensile deformation and in the changes observed during thermal analyses. These observations were analysed in terms of the constituent fibroin sequences, which in B. mori are predicted to produce heterogeneous structures, whereas the strictly modular repeats of the saturniid sequences are hypothesized to produce structures that respond in a concerted manner. Within saturniid fibroins, thermal stability was found to correlate with the abundance of poly-alanine residues, whereas differences in fibre extensibility can be related to varying ratios of GGX motifs versus bulky hydrophobic residues in the amorphous phase.

Spider silks are among the toughest known materials and thus provide models for renewable, biodegradable, and sustainable biopolymers. However, the entirety of their diversity still remains elusive, and silks that exceed the performance limits of industrial fibers are constantly being found. We obtained transcriptome assemblies from 1098 species of spiders to comprehensively catalog silk gene sequences and measured the mechanical, thermal, structural, and hydration properties of the dragline silks of 446 species. The combination of these silk protein genotype-phenotype data revealed essential contributions of multicomponent structures with major ampullate spidroin 1 to 3 paralogs in high-performance dragline silks and numerous amino acid motifs contributing to each of the measured properties. We hope that our global sampling, comprehensive testing, integrated analysis, and open data will provide a solid starting point for future biomaterial designs.

An artificial spinning system using regenerated silk fibroin solutions is adopted to produce high-performance silk fibers. In previous studies, alcohol-based agents, such as methanol or ethanol, were used to coagulate silk dope solutions, producing silk fiber with poor mechanical properties compared with those of native silk fibers. The alcohol-based coagulation agents induce rapid β-sheet crystallization of the silk molecules, which inhibits subsequent alignment of the β-sheet crystals. Here, we induce gradual β-sheet formation to afford adequate β-sheet alignment similar to that of native silk fiber. To this aim, we developed an amorphous silk fiber spinning process that prevents fast β-sheet formation in silk molecules by using tetrahydrofuran (THF) as a coagulation solvent. In addition, we apply postdrawing to the predominantly amorphous silk fibers to induce β-sheet formation and orientation. The resultant silk fibers showed a 2.5-fold higher extensibility, resulting in 1.5-fold tougher silk fibers compared with native Bombyx mori silk fiber. The amorphous silk fiber spinning process developed here will pave the way to the production of silk fibers with desired mechanical properties.

Native silk fibers are known to demonstrate excellent mechanical properties such as high strength and ductility. However, regenerated silk material has not yet been used as a tough structural material in our everyday life. To recreate the mechanical properties with regenerated silk material, the network structure and hydration state of silk materials are studied and optimized in this study. This is the first to demonstrate the effect of chemical and physical cross-links in hydrated and dehydrated silk materials, namely, silk hydrogels and resins. Mild hydration conditions (relative humidity 20-60%) realizes tough and strong silk materials with chemical and physical cross-links. In the case of relatively high concentrations of silk molecules, contributions to the high strength and toughness of silk-based materials are considered to come not only from β-sheet cross-links and chemical dityrosine links but also from entanglements and assembly via the hydrophobic interactions of silk molecules. In addition, dehydration treatment does not disturb the biodegradability of the silk resins in natural environments. Based on the overall results, the silk resins with controlled network structures and hydration state have successfully achieved the highest toughness possible for a bulk silk material while maintaining favorable biodegradability.

Silk fibroin (SF) is a fascinating natural biomaterial that exhibits remarkable mechanical properties and biocompatibility. Meanwhile, biological adhesive materials have gathered much attention as biomedical and ecofriendly materials as a result of their characteristic properties. Herein, we report the excellent adhesive function of enzymatically modified SF. The tyrosine residues of SF were successfully converted to the dihydroxy-l-phenylalanine (DOPA) unit using tyrosinase as a biocatalyst. The content of DOPA was evaluated by amino acid composition analysis. Adhesive functions of DOPA-modified SF (DOPA-SF) among several material surfaces including mica, paper, polypropylene, wood, and silk film were elucidated by lap shear tests. Fourier transform infrared measurements demonstrated that the adhesion strength of DOPA-SF was not directly related to the β-sheet formation of silk molecules. This ecofriendly and facile method offers a new perspective for fabricating natural adhesive materials for various application areas.