Controllable self-assembly of tyrosine-rich triblock peptides into robust collagen mimetic bioscaffolds for aging skin rejuvenation.

Skin aging, a complex physiological process characterized by alterations in skin structure and function, seriously affects human life. Collagen holds considerable potential in aging skin treatment, while animal-derived collagen poses risks of pathogen transmission. Self-assembled peptides have garnered increasing attention in creating collagen mimetic materials; however, previous reported self-assembled peptides rely on vulnerable non-covalent interactions or lack the capability of controlling morphology and incorporating functional motifs, limiting their ability to mimic collagen structure and function. We have herein created a controllable tyrosine-rich triblock peptide system capable of self-assembling into robust collagen mimetic bioscaffolds for rejuvenating aging skin. Through ruthenium-mediated crosslinking, these peptides self-assemble into well-defined nanospheres or collagen-mimetic scaffolds, precisely regulated by the triple-helical structure and tyrosine distribution. The self-assembled collagen mimetic scaffolds exhibit outstanding resistances to various solvents and pH conditions. The integrin-binding motif has been incorporated into the triple helical block without disrupting their assembly, while endowing them with superior bioactivities, effectively promoting cell adhesion and proliferation.