Recombinant collagen hydrogels induced by disulfide bonds.

ABSTRACT: With the characteristics of low toxicity and biodegradability, recombinant collagen-like proteins have been chemically and genetically engineered as a scaffold for cell adhesion and proliferation. However, most of the existing hydrogels crosslinked with peptides or polymers are not pure collagen, limiting their utility as biomaterials. A major roadblock in the development of biomaterials is the need for high purity collagen that can self-assemble into hydrogels under mild conditions. In this work, we designed a recombinant protein, S-VCL-S, by introducing cysteine residues into the Streptococcus pyogenes collagen-like protein at both the N-and C-termini of the collagen with a trimerization domain (V) and a collagen domain (CL). The S-VCL-S protein was properly folded in complete triple hel

SUBMITTER: Wang J 

PROVIDER: S-EPMC9544300 | biostudies-literature | 2022 Nov

REPOSITORIES: biostudies-literature