Flow-induced protein chain deformation, segmental orientation, and phase separation in native silk feedstock

The ability of many arthropods to spin silk and its many uses bear testament to its importance in Nature. Despite over a century of research, however, the spinning process is still not fully understood. While it is widely accepted that flow and chain alignment may be involved, the link to protein gelation remains obscure. Using combinations of rheology, polarized light imaging, and infrared spectroscopy to probe different length scales, this work explored flow-induced gelation of native silk feedstock from Bombyx mori larvae. Protein chain deformation, orientation, and microphase separation were observed, culminating in the formation of antiparallel β-sheet structures while the work rate during flow appeared as an important criterion. Moreover, infrared spectroscopy provided direct observations suggesting a loss of protein hydration during flow-induced gelation of fibroin in native silk feedstock, which is consistent with recently reported hypotheses.