Self-assembly behavior of the keratose proteins extracted from oxidized Ovis aries wool fibers.

Water soluble keratose proteins were obtained from an Ovis Aries wool using peracetic acid oxidation. The wool samples and the extracted keratose proteins were characterized by using FTIR, XRD, SEM and TGA techniques. Fractions of α-keratose (MW = 43-53 kDa) along with protein species with molecular weights between 23 kDa and 33 kDa were identified in the SDS-PAGE analysis result of the extracted protein mixture. DLS and AFM experiments indicated that self-assembled globular nanoparticles with diameters between 15 nm and 100 nm formed at 5 mg/ml keratose concentration. On the other hand, upon incubation of 10 w % keratose solutions at 37 °C and 50 °C, interconnected keratose hydrogels with respective storage modulus (G') values of 0.17 ±â€¯0.03 kPa and 3.7 ±â€¯0.5 kPa were obtained. It was shown that the keratose hydrogel prepared at 37 °C supported L929 mouse fibroblast cell proliferation which suggested that these keratose hydrogels could be promising candidates in soft tissue engineering applications.