论文标题
哺乳动物组织源对紫外固定I型胶原水凝胶网络的分子和宏观特性的影响
Effect of Mammalian Tissue Source on the Molecular and Macroscopic Characteristics of UV-Cured Type I Collagen Hydrogel Networks
论文作者
论文摘要
I型胶原蛋白的组织来源对于确保新医疗设备原型的可伸缩性和调节的临床翻译至关重要。但是,选择符合上述要求并符合新制造路线的商业胶原蛋白来源是具有挑战性的。这项研究调查了从三种不同的哺乳动物组织中提取的I型胶原蛋白对新型UV固定胶原水凝胶的分子和宏观特性的作用。胃蛋白溶解的牛atelocollagen(BA)和胃蛋白酶溶解的猪腹膜肌氨酸(PA)被选为与安全风险不同的市售原材料,并与内部酸酸提取的I型I型胶原蛋白胶原(CRT)相比。所有原材料都显示出I型胶原蛋白的典型二分法和电泳特性,同时在PA样品上测量了赖氨酸含量的显着降低。在与4-乙烯基苯基氯化物(4VBC)的共价功能化后,BA和CRT产物产生了可比较的紫外线固定水凝胶,平均凝胶含量显着增加(g> 97 wt。%),而牛肝菌变异却显示了最高的肿胀比(SR = 2224 +//--242 W.%。 +/- 2 kPa)。总的来说,这些结果支持将牛组织用作I型胶原蛋白的化学可行来源,以实现具有竞争性机械性能和共价网络体系结构的紫外线固定水凝胶。
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.