Animal Extraction
Risk of viral transmission and immunogenicity; poor solubility; hard to modify specifically; has a triple-helix structure
The third generation of biomimetic collagen after animal-extracted and recombinant collagen
World's first triple-helix biomimetic collagen ECM
Risk of viral transmission and immunogenicity; poor solubility; hard to modify specifically; has a triple-helix structure
Scalable manufacturing; proline is hard to hydroxylate site-specifically, lacking hydroxyproline; usually no triple-helix structure
Latest-generation collagen; biomimetic, non-immunogenic, easy to handle and functionalize; stable triple-helix structure
Materials Science
Amino Acid Model Schematic
Amino acid sequences precisely recreate the native collagen Gly-X-Y repeat. 300 kV cryo-EM confirms stable self-assembled fiber bundles—from a single peptide chain to nanoscale fiber networks, from aqueous polymerization to self-crosslinking gels. LivingPHOENIX has ended both the risks of animal extraction and the structural gaps of recombinant collagen.
Animal-free. Virus-free. Non-immunogenic. Survives 121°C moist-heat terminal sterilization. Epithelialization up to 12× bovine collagen and 8.13× recombinant collagen.
This is not an upgrade of recombinant collagen—it is collagen coming home. Regeneration starts with the right structure.
First high-resolution fiber-bundle imaging of biomimetic collagen worldwide
TITAN KRIOS G4 Cryo-EM
Using the 300 kV cryo-TEM TITAN KRIOS G4, we captured the self-assembled collagen morphology of multiple POGMENT biomimetic collagen batches.
Built on triple-helix biomimetic collagen, five material platforms—liquid, self-crosslinked, co-crosslinked, smart gelation, and biomimetic composites—serve medical devices, cosmetics, and tissue regeneration.