Silk fibroin is a multisegment natural protein composed of a heavy (H) chain, a light (L) chain and a P25 glycoprotein chain. Herein, we developed a dialysis separation technique under reducing conditions to break the disulfide bond between the H-chain and L-chain and remove the low-molecular-weight portions of the protein. Thus, a high-molecular-weight silk fibroin polypeptide (HSF) material was obtained. SDS-PAGE electrophoresis showed that the molecular weight of HSF was over 80 kDa, similar to the size of the silk fibroin H-chain. Amino acid analysis result demonstrated that the amino acid composition of HSF was almost identical to that of H-chain composition. Importantly, the HSF material obtained has a high surface activity, which can reduce the surface tension of water to below 20 mN/m; at high temperature and high concentration, it can also form a unique nanofibrous network with a lamellar crystalline structure. HSF can further form a rod-shaped structure in a strong polar environment and become a star-shaped fibrous network in a weak polar environment. When the pH value of HSF solution was adjusted from 6 to 8, a structural transition from a folded crank sheet-like structure with micellar beads to a ring-like fibrous structure was observed. During the conversion of HSF from colloidal particles to nanofibers, its molecular conformation also transformed from random coils to β-sheets. These tunable properties indicate that HSF materials have a wide range of applications in biomedical and green chemistry fields.
All Science Journal Classification (ASJC) codes
- Biomedical Engineering
- Biochemistry, medical