Disulfide-Orthogonalized Collagen Hydrogels Balance D-Periodic Assembly and Network Formation for Bone Repair

Here, we describe de novo collagen hydrogel designs and define the impacts of organization and crosslinking among modular peptide fragments on secondary structure, supramolecular interactions, hierarchical self-assembly, and their influence on microstructure, mechanics, and function of the macroscopic hydrogel.

By strategically incorporating disulfide bonds into the adhesive and functional-driver modules of the collagen peptide fragments, we could design supramolecular interactions that promote hydrogel formation while retaining the secondary structure and hierarchical self-assembly of biomimetic D-periodic fibers. Additionally, these synthetic fibers could promote osteoblast differentiation and femoral fracture repair with comparable efficacy to natural collagen in rats.