No abstract

Smart hydrogels with versatile properties, including a tunable gelation time, nonswelling attributes, and biocompatibility, are in great need in the biomedical field. To meet this urgent demand, we explored novel biomaterials with the desired properties from sessile marine organisms. To this end, a novel protein, Sbp9, derived from scallop byssus was extensively investigated, which features typical epidermal growth factor-like (EGFL) multiple repetitive motifs. Our current work demonstrated that the key fragment of Sbp9 (calciumbinding domain (CBD) and 4 EGFL repeats (CE4)) was able to form a smart hydrogel driven by noncovalent interactions and facilitated by disulfide bonds. More importantly, this smart hydrogel demonstrates several desirable and beneficial features, which could offset the drawbacks of typical protein-based hydrogels, including (1) a redoxresponsive gelation time (from <1 to 60 min); (2) tunable mechanical properties, nonswelling abilities, and an appropriate microstructure; and (3) good biocompatibility and degradability. Furthermore, proof-of-concept demonstrations showed that the newly discovered hydrogel could be used for anticancer drug delivery and cell encapsulation. Taken together, a smart hydrogel inspired by marine sessile organisms with desirable properties was generated and characterized and demonstrated to have extensive applicability potential in biomedical applications, including tissue engineering and drug release.

Antioxidant biomaterials have attracted much attention in various biomedical fields because of their effective inhibition and elimination of reactive oxygen species (ROS) in pathological tissues. However, the difficulty in ensuring biocompatibility, biodegradability and bioavailability of antioxidant materials has limited their further development. Novel bioavailable antioxidant materials that are derived from natural resources are urgently needed. Here, an integrated multi-omics method was applied to fabricate antioxidant biomaterials. A key cysteine-rich thrombospondin-1 type I repeat-like (TSRL) protein was efficiently discovered from among 1262 adhesive components and then used to create a recombinant protein with a yield of 500 mg L −1 . The biocompatible TSRL protein was able to self-assemble into either a water-resistant coating through Ca 2+ -mediated coordination or redox-responsive hydrogels with tunable physical properties. The TSRL-based hydrogels showed stronger 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical scavenging rates than glutathione (GSH) and ascorbic acid (Aa) and protected cells against external oxidative stress significantly more effectively. When topically applied to mice skin, TSRL alleviated epidermal hyperplasia and suppressed the degradation of collagen and elastic fibers caused by ultraviolet radiation B (UVB) irradiation, confirming that it enhanced antioxidant activity in vivo . This is the first study to successfully characterize natural antioxidant biomaterials created from marine invertebrate adhesives, and the findings indicate the excellent prospects of these biomaterials for great applications in tissue regeneration and cosmeceuticals.