SUMMARY
Silk fibroin (SF) has been continuously explored as a biomaterial due to its biocompatibility, tunability, and self-healing properties. In this work, we present a novel approach to the modification of bacterial cellulose (BC) with SF ß-sheet dominant structures induced via ultrasonication. Secondary structure analysis through infrared spectroscopy, thioflavin T assay, and circular dichroism spectropolarimetry revealed a conversion of silk I to silk II structures within the protein mixture. Cold field emission scanning electron microscope images revealed the tightly packed fibers coated with the protein. Thermogravimetric curves demonstrated higher resistance to temperature degradation supplemented by broader and flatter DSC curves attributed to the highly bonded and dense composite. Successful conversion of amide I to amide II and amide III allowed for the more stable ß-crystals to contribute to a more thermodynamically stable double-network hydrogel. The conversion of silk I to silk II structures offers a viable and highly biocompatible material that is both thermodynamically and biochemically stable for various potential biomedical applications.