Abstract
The tissue source of type I collagen is critical to ensure scalability and regulation-friendly clinical translation of new medical device prototypes. However, the selection of a commercial source of collagen that fulfils both aforementioned requirements and is compliant with new manufacturing routes is challenging. This study investigates the effect that type I collagen extracted from three different mammalian tissues has on the molecular and macroscopic characteristics of a new UV-cured collagen hydrogel. Pepsin-solubilised bovine atelocollagen (BA) and pepsin-solubilised porcine atelocollagen (PA) were selected as commercially available raw materials associated with varying safety risks and compared with in-house acid-extracted type I collagen from rat tails (CRT). All raw materials displayed the typical dichroic and electrophoretic characteristics of type I collagen, while significantly decreased lysine content was measured on samples of PA. Following covalent functionalisation with 4-vinylbenzyl chloride (4VBC), BA and CRT products generated comparable UV-cured hydrogels with significantly increased averaged gel content (G ≥ 97 wt.%), while the porcine variants revealed the highest swelling ratio (SR = 2224 ± 242 wt.%) and an order of magnitude reduction in compression modulus (Ec = 6 ± 2 kPa). Collectively, these results support the use of bovine tissues as a chemically viable source of type I collagen for the realisation of UV-cured hydrogels with competitive mechanical properties and covalent network architectures.
Highlights
Type I collagen is a major protein component of connective tissues and is largely found in tendon, cartilage, ligament, and skin [1,2]
Collagen samples deriving from three different mammalian tissues were employed as building blocks for the creation of UV-cured functionalised hydrogels (Figure 1)
Type I collagens from three mammalian sources were covalently functionalised with 4-vinylbenzyl chloride (4VBC) to form UV-cured hydrogels, aiming to develop relationships between the molecular characteristics of the raw material and the macroscopic properties of the resulting hydrogel
Summary
Type I collagen is a major protein component of connective tissues and is largely found in tendon, cartilage, ligament, and skin [1,2]. The selection of the tissue source for the extraction of the collagen raw material has increasingly been identified as a key aspect to ensure reproducibility, scalable development, and clinical translation of new medical device prototypes. This is dictated by (i) the animal-induced variation in the chemical composition of collagen; (ii) the recent implementation of the new medical device regulation in the EU [15,16]; and (iii) the increasing efforts of academic institutions worldwide to pursue technology innovation and bridge the gap between the bench and bedside [17]
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