Over the last two decades, fibroin, a protein derived from silk, has captured the researchers attention because of the peculiar combination of properties such as mechanical strength and toughness, biocompatibility, biodegradability, thermal stability, and easy processability. Regenerated silk fibroin has been used as a functional biomaterial, adopted when a positive interaction with living tissue is required.
In a recent research published in Advanced Functional Materials, a group of researchers from the Department of Industrial Engineering have developed a new method to produce a silk derived bioplastic.
The low-temperature high-pressure sintering approach adopted allows obtaining a bulk solid silk in minutes and to integrate thermally degradable molecules.
The research was conducted starting by the idea of integrating a fast method suitable for a large-scale production and a low temperature fundamental to incorporate thermally degradable molecules such as enzymes and bioactive compounds into the solid matrix.
The solution proposed by Alessio Bucciarelli (PhD student) under the supervision of prof. Devid Maniglio, Antonella Motta, and Alberto Quaranta, and in collaboration with Silvia Chiera (PhD student) and Vamsi K. Yadavally (Virginia Commonwealth University), consists in a high pressure compression at 40 °C of a protein pellet characterized by an intrinsic low degree of crystallinity. This procedure can trigger the transformation of the initial friable pellet into a mechanically resistant, continuous material.
The group, for the first time, demonstrate how the transition from a fibroin sponge to a hard, bulk material takes place, explaining the role of the protein’s secondary structure and guided by the viscous flow of the proteins.
Researcher are convinced that this production technique, in the future, could be usable for developing resorbable biomedical devices.
The full paper is available at the following link: