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Biomacromolecules ; 22(10): 4337-4346, 2021 10 11.
Article in English | MEDLINE | ID: mdl-34515486

ABSTRACT

Silk contains an adhesive glycoprotein, silk sericin, in which silk fibroins can be enfolded and chemically stabilized. Silk sericin is gaining importance as the material for the creation of functional bioscaffolds. However, the assembly of silk sericin is generally limited to the blend of polymers or proteins due to its inherent poor mechanical strength. Here, we report a simple macroscopic controlled assembly of silk sericin fibers based on their secondary structure via wet-spinning. In addition, plasticization of silk sericin using glycerol immobilized with glutaraldehyde was found to induce dimensional stability, affording stable linear fibers with self-adhesion. Furthermore, cyclo-phenylalanine nanowires were incorporated into the silk sericin dope for a practical demonstration of their potential in artificial silk production with superstructure formation. The physicochemical characteristics of the spun fibers have also been elucidated using Fourier-transform infrared spectroscopy, electron microscopy, tensile test, differential scanning calorimetry, and 2D X-ray diffraction.


Subject(s)
Fibroins , Sericins , Protein Structure, Secondary , Silk , Spectroscopy, Fourier Transform Infrared
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