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Introduction to Collagen
Collagen is the main structural protein in human tissues and organs. It is composed of procollagen, and each procollagen molecule consists of three α-helical peptide chains twisted together into a characteristic triple-helix structure. Multiple collagen molecules further intertwine to form collagen fibers.
Today, dozens of collagen types have been identified, accounting for about 30–40% of the total protein in the human body, making it one of the most essential structural materials. Beyond its biological role, collagen has also gained great attention in medical and cosmetic fields. It not only enhances skin elasticity but also promotes wound healing, which makes it a key ingredient in aesthetic medicine and related industries.
Safety Requirements for Collagen
With the rapid expansion of the collagen market, expectations for product safety and quality have risen significantly. Traditional collagen extraction methods have inherent limitations. Collagen derived from animal connective tissues carries potential risks of zoonotic contamination. Meanwhile, collagen produced in E. coli or yeast expression systems often suffers from repetitive amino acid sequences and lacks essential hydroxylation modifications. As a result, its triple-helix structure tends to be unstable at room temperature, sometimes existing only as single linear chains.
In contrast, recombinant humanized collagen expressed in CHO cells can faithfully reproduce the native triple-helix structure of natural collagen. Even under room temperature, its helical structure remains stable and compact. This makes it an ideal material for applications in healthcare, aesthetics, and medical devices, offering high market potential.
However, since CHO cells are of animal origin, recombinant humanized collagen produced in this system carries an inherent risk of viral contamination. Therefore, viral clearance validation must be performed in accordance with the ICH Q5A (R2) Guideline on viral safety evaluation of biotechnology products derived from cell lines of human or animal origin. Among available viral reduction strategies, virus filtration offers an effective and robust means of viral removal without altering the physicochemical properties of collagen. Nevertheless, potential viral risks originating from the animal-derived cell substrate must be tightly controlled through a validated and stringent viral clearance process.
Case Study of Virus Removal Filtration in the Production Process of Recombinant Humanized Collagen
1. Comparison of Viruclear PDT (Depth Filter), Viruclear PNY (Nylon Membrane), and CorevitalTM SMDA (PVDF):
Protein solution: ~300 kDa, concentration 0.2 g/L
Prefilter: PDT virus removal depth filter, PNY nylon virus removal prefilter, and SMDA sterilizing-grade filter
Filtration pressure: 1.0 bar
Experimental Conclusion:
It is recommended to use the SMDA sterilizing-grade filter as the prefilter for viral clearance.
2. Performance of Virus Removal Filters at Different Protein Concentrations:
Protein solution: The same recombinant humanized collagen sample was diluted to 0.1 g/L and 0.3 g/L.
Prefiltration: Each sample was prefiltered using the SMDA sterilizing-grade filter.
Filtration pressure: 30 psi
Virus removal filters tested: VF Plus, VF Plus X, RC H
A: 0.1 g/L Protein Solution
B: 0.3 g/L Protein Solution
Experimental Conclusion:
- For low-concentration solutions (below 0.1 g/L), the Viruclear VF Plus X filter is recommended for viral clearance.
- For higher-concentration solutions (0.1–0.3 g/L and above), the Viruclear RC H filter is recommended.
In summary, considering the virus removal requirements in recombinant humanized collagen production, Cobetter’s viral clearance products offer a comprehensive and reliable solution.
