Reinforcement of Fibrillar Collagen Hydrogels with Bioorthogonal Covalent Crosslinks.

ABSTRACT: Bioorthogonal covalent crosslinking stabilizes collagen type I hydrogels, improving their structural integrity for tissue engineering applications with encapsulated living cells. The chemical modification required for crosslinking, however, interferes with the fibrillar nature of the collagen, leading instead to an amorphous network without fibers. We demonstrate an approach to perform bioconjugation chemistry on collagen with controlled localization such that the modified collagen retains its ability to self-assemble into a fibrillar network while also displaying functional groups for covalent crosslinking with bioorthogonal click chemistry. The collagen matrix is formed through a sequential crosslinking process, in which the modified collagen first physically assembles into fibers and th

SUBMITTER: Brunel LG 

PROVIDER: S-EPMC12715433 | biostudies-literature | 2025 Jul

REPOSITORIES: biostudies-literature