Laccase-mediated formation of hydrogels based on silk-elastin-like protein polymers with ultra-high molecular weight.

As artificial extracellular matrix-like materials, silk-elastin-like protein (SELP) hydrogels, with excellent mechanical properties, high tunability, favorable biocompatibility, and controlled degradability, have become an important candidate in biomedical materials. In this study, SELP is composed of silk-like (GAGAGS) and elastin-like (GXGVP) tandem repeats, in which X residues are set as tyrosine and lysine. Furthermore, SELP polymers are prepared via SpyTag/SpyCatcher. To explore a gentler and more efficient enzymatic crosslinking method, an innovative method was invented to apply laccase to catalyze the formation of SELP hydrogels. Gelation could be successfully achieved in 2-5 min . SELP hydrogels mediated by laccase had the characteristic of low swelling rate, which could maintain a relatively stable shape even when immersed in water, and hence had the potential to be further developed into injectable biomaterials. Additionally, SELP hydrogels cross-linked by laccase showed excellent biocompatibility verified by L929 and HEK 293 T cells with cell viability >93.8 %. SELP hydrogels also exhibit good properties in sustained drug release and cell encapsulation in vitro. This study demonstrates a novel method to construct SELP hydrogels with excellent biocompatibility and expands the possibility of SELP-based material applications in biomedical fields.