Probing the Interplay of Protein Self-Assembly and Covalent Bond Formation in Photo-Crosslinked Silk Fibroin Hydrogels.

ABSTRACT: Covalent crosslinking of silk fibroin via native tyrosine residues has been extensively explored; however, while these materials are very promising for biomedical, optical, soft robotics, and sensor applications, their structure and mechanical properties are unstable over time. This instability results in spontaneous silk self-assembly and stiffening over time, a process that is poorly understood. This study investigates the interplay between self-assembly and di-tyrosine bond formation in silk hydrogels photo-crosslinked using ruthenium (Ru) and sodium persulfate (SPS) with visible light. The effects of silk concentration, molecular weight, Ru/SPS concentration, and solvent conditions are examined. The Ru/SPS system enables rapid crosslinking, achieving gelation within seconds and incorpo

SUBMITTER: Tran HA 

PROVIDER: S-EPMC12019910 | biostudies-literature | 2025 Apr

REPOSITORIES: biostudies-literature