Engineering High Strength and Super‐Toughness of Unfolded Structural Proteins and their Extraordinary Anti‐Adhesion Performance for Abdominal Hernia Repair

The utility of unfolded structural proteins with diverse sequences offers multiple potentials to create functional biomaterials. However, it is challenging to overcome their structural defects for the development of biological fibers with a combination of high strength and high toughness. Herein, robust fibers from a recombinant unfolded protein consisting of resilin and supercharged polypeptide are fabricated via wet-spinning approaches. Particularly, the highly ordered structures induced by supramolecular complexation significantly improve the fiber's mechanical performance. In contrast to chemical fibers with high strength and low toughness (or vice versa), the present fibers demonstrate exceptional high strength and super-toughness, showing a breaking strength of ≈550 MPa and a toughness of ≈250 MJ m-3 , respectively, surpassing many polymers and artificial protein fibers. Remarkably, the outstanding biocompatibility and superior mechanical properties allow application of the constructed fiber patches for efficient abdominal hernia repair in rat models. In stark contrast to clinical patches, there is no observed tissue adhesion by this treatment. Therefore, this work provides a new type of engineered protein material for surgical applications.