常见哺乳动物源胶原蛋白的提取及其性能表征

Extraction and characterization of common mammalian collagen

为了评价不同哺乳动物源胶原蛋白理化性能和生物学性能,采用酶法提取从常见哺乳动物猪、鼠、牛中提取胶原蛋白,并对其提取的胶原蛋白氨基酸组成、理化性能和生物相容性进行评价。结果表明,不同来源胶原蛋白氨基酸组成及含量不同;FT-IR图谱显示所提取3种胶原蛋白都较好地维持其三螺旋结构;TG结果表明3种胶原蛋白具有较为相似的热行为,其中猪皮胶原(pig skin collagen,PS-col)对热降解具有更高的稳定性;SEM照片显示鼠尾胶原膜(rat tail collagen,RT-col)具有微粗糙结构表面,猪皮胶原膜表面较为光滑,牛跟腱胶原膜(bovine tendon collagen,BT-col)适中;AFM观察到3种胶原蛋白都呈现胶原纤维束状结构,但不同来源胶原蛋白形成胶原纤维存在差异性;力学性能测试表明牛跟腱胶原能够较好抵抗外界作用力且材料柔性好,猪皮胶原杨氏模量最大,较其它二者不易发生形变,鼠尾胶原力学性能介于二者之间。体外细胞实验结果表明,3种胶原蛋白都具有良好的生物相容性。为优选以胶原基为生物材料满足不同需求匹配提供更多参考。

In order to evaluate the physical, chemical and biological properties of collagen from different mammalian sources, collagen was enzymatically extracted from common mammalian pigs, rats and bovine, and its amino acid composition, structure, morphology and biological properties were evaluated. The results showed that the amino acid composition and content of collagen from different sources were different. The FT-IR spectrum showed that the three collagens were well maintained in their three-helix structure. The TG results showed that the three collagens had similar thermal behavior, and the pig skin collagen (PS-col) had higher stability to thermal degradation. The SEM photograph showed that the rat tail collagen (RT-col) had a slightly roughest surface, the surface of the pig skin collagen was the smoothest, and the bovine tendon collagen (BT-col) was moderate. The AFM observed that all three collagens showed a collagen fiber bundle structure, but there were differences in the formation of collagen fibers from different sources of collagen. The mechanical properties test showed that the bovine tendon collagen could resist the external force and the material flexibility was easy to deform. The Young's modulus of the pig skin collagen was the largest, which was less likely to be deformed than the other two, and the rat tail collagen was between the two. In vitro cell experiments showed that all three collagens had good biocompatibility. This study provided more reference for the selection of collagen-based biomaterials to meet different needs.