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Early insights into the unique structure and properties of native silk suggested that β-sheet nanocrystallites in silk would degrade prior to melting when subjected to thermal processing. Since then, canonical approaches for fabricating silk-based materials typically involve solutionderived processing methods, which have inherent limitations with respect to silk protein solubility, stability in solution, and time and cost efficiency. Here we report a thermal processing method for the direct solid-state molding of regenerated silk into bulk 'parts' or devices with tunable mechanical properties. At elevated temperature and pressure, regenerated amorphous silk nanomaterials with ultralow β-sheet content undergo thermal fusion via molecular rearrangement and self-assembly assisted by bound water to form a robust bulk material that retains biocompatibility, degradability and machinability. This technique reverses presumptions about the limitations of direct thermal processing of silk into a wide range of new material formats and composite materials with tailored properties and functionalities. Users may view, print, copy, and download text and data-mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use:

Silkworm silk has attracted considerable attention in recent years due to its excellent mechanical properties, biocompatibility, and promising applications in biomedical sector. However, a clear understanding of the molecular structure and the relationship between the excellent mechanical properties and the silk protein sequences are still lacking. This study carries out a thorough comparative structural analysis of silk fibers of four silkworm species ( Bombyx mori, Antheraea pernyi, Samia cynthia ricini, and Antheraea assamensis). A combination of characterization techniques including scanning electron microscopy, mechanical test, synchrotron X-ray diffraction, Fourier transform infrared spectroscopy (FTIR), and NMR spectroscopy was applied to investigate the morphologies, mechanical properties, amino acid compositions, nanoscale organizations, and molecular structures of various silkworm silks. Furthermore, the structure-property relationship is discussed by correlating the molecular structural features of silks with their mechanical properties. The results show that a high content of β-sheet structures and a high crystallinity would result in a high Young's modulus for silkworm silk fibers. Additionally, a low content of β-sheet structures would result in a high extensibility.

As a biomaterial, silk presents unique features with a combination of excellent mechanical properties, biocompatibility, and biodegradability. The biodegradability aspects of silk biomaterials, especially with options to control the rate from short (days) to long (years) time frames in vivo, make this protein-based biopolymer a good candidate for developing biodegradable devices used for tissue repairs and tissue engineering, as well as medical device implants. Silk materials, including native silk fibers and a broad spectrum of regenerated silk materials, have been investigated in vitro and in vivo to demonstrate degradation by proteolytic enzymes. In this Review, we summarize the findings on these studies on the enzymatic degradation of Bombyx mori (B. mori) silk materials. We also present a discussion on the factors that dictate the degradation properties of silk materials. Finally, in future perspectives, we highlight some key challenges and potential directions toward the future study of the degradation of silk materials.