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The tissue source of type I collagen is critical to ensure scalability andregulation-friendly clinical translation of new medical device prototypes.However, the selection of a commercial source of collagen that fulfils bothaforementioned requirements and is compliant with new manufacturing routes ischallenging. This study investigates the effect that type I collagen extractedfrom three different mammalian tissues has on the molecular and macroscopiccharacteristics of a new UV-cured collagen hydrogel. Pepsin-solubilised bovineatelocollagen (BA) and pepsin-solubilised porcine atelocollagen (PA) wereselected as commercially available raw materials associated with varying safetyrisks and compared with in-house acid-extracted type I collagen from rat tails(CRT). All raw materials displayed the typical dichroic and electrophoreticcharacteristics of type I collagen, while significantly decreased lysinecontent was measured on samples of PA. Following covalent functionalisationwith 4-vinylbenzyl chloride (4VBC), BA and CRT products generated comparableUV-cured hydrogels with significantly increased averaged gel content (G > 97wt.%), 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 bovinetissues as a chemically viable source of type I collagen for the realisation ofUV-cured hydrogels with competitive mechanical properties and covalent networkarchitectures.

Effect of Mammalian Tissue Source on the Molecular and Macroscopic Characteristics of UV-Cured Type I Collagen Hydrogel Networks