Abstract:[Objective] The aim of this study is to address the insolubility of elastin derived from animals and the aggregation of recombinant elastin-like proteins, and to enhance the elastin potential application in functional foods. [Method] In view of the above problems, resilin 16 (R16) derived from insects, immunoglobulin G domain B1 (GB1) from Streptococcus, and the Ure2 sequence of aa 1~80 Ure2(1-80) from Saccharomyces cerevicae were linked with the RGD sequence (a binding site of cells that promote cell adhesion) to construct the soluble supramolecular elastin. The cytotoxicity of the supramolecular elastin to C2C12 cells as well as its biosafety was evaluated. Furthermore, the supramolecular elastin was compared with hyaluronic acid (HA) and pigskin collagen in terms of the cell proliferation-promoting effect and antioxidant capacity. [Result] The supramolecular elastin had no toxic effect on cells and did not induce obvious inflammation after subcutaneous injection, demonstrating high biosafety. The self-assembled fibril promoted cell proliferation, and it showcased stronger scavenging ability against four kinds of free radicals and protective effect against H2O2-induced damage of L929 cells than HA and pigskin collagen. [Conclusion] The obtained supramolecular elastin has high biosafety, cell proliferation-promoting effect, and antioxidant capacity, serving as a new material for the development of functional food.
