胶原交联的改性研究进展(二)

Research Progress on Modification of Collagen Crosslinking(2)

胶原蛋白作为一种在各类结缔组织中广泛存在的重要结构蛋白,其独特的三螺旋结构和形成交联网络的能力,为其提供了显著的机械强度和耐久性。通过不同的交联方法,特别是化学交联,可以显著改善胶原蛋白的物理和化学性质,从而拓宽其在医学、食品工业、环保和化妆品等领域的应用范围。各种交联剂,包括戊二醛、EDC/NHS体系、酚酸、京尼平以及纳米粒子等,均显示出增强胶原蛋白力学性能、热稳定性和抗酶降解能力的潜力。这些性能的提升,为胶原蛋白基材料的生物医学应用,如血管移植、软骨修复、器官再生、角膜修复以及在食品包装和保湿化妆品中的应用,提供了重要支持。

Collagen,as a vital structural protein widely present in various connective tissues,derives significant mechanical strength and durability from its unique triple helix structure and ability to form crosslinked networks.Various crosslinking methods,particularly chemical crosslinking,significantly enhance the physical and chemical properties of collagen,thereby expanding its application in medical,food industry,environmental protection,and cosmetics fields.Various crosslinking agents,including glutaraldehyde,EDC/NHS system,phenolic acids,genipin,and nanoparticles,demonstrate potential in enhancing collagen's mechanical properties,thermal stability,and resistance to enzymatic degradation.These enhanced characteristics provide crucial support for biomedical applications of collagen-based materials,such as vascular grafts,cartilage repair,organ regeneration,corneal repair,as well as applications in food packaging and moisturizing cosmetics.