Collagen Methacryloyl Photoresins: Collagen Source, Methacrylation, Triple-Helix State, Low-Temperature DLP, Hydration, Enzymatic Degradation and Qualification

Primary evidence shows that type-I collagen can be methacrylated while retaining fibrillar self-assembly and enzymatic degradability, but source, extraction, solubilisation, methacrylation and neutralisation remain material-defining. Gaudet and Shreiber reported rapid 365 nm photocrosslinking, a five-fold storage-modulus increase and state-dependent collagenolytic resistance for one collagen methacrylamide route. Han et al. later combined extracted ColMA with PEGDA for DLP printing, creating a hybrid rather than a neat collagen network. This review separates collagen identity, triple-helix/fibril state, derivatisation, formulation, low-temperature handling, optical processing, hydration, mechanics, collagenase degradation and biological evidence, and defines minimum qualification gates.

3Dresyns Engineering Review ER-122, version 0.2. Provider-neutral technical review. The deposited PDF is controlled by its exact SHA-256 in the release manifest.