Madhan B, Subramanian V, Rao J Raghava, Nair Balachandran Unni, Ramasami T
Centre for Human and Organizational Resources Development, Central Leather Research Institute, Adyar, Chennai 600 020, India.
Int J Biol Macromol. 2005 Oct 30;37(1-2):47-53. doi: 10.1016/j.ijbiomac.2005.08.005. Epub 2005 Sep 23.
Collagen, a unique connective tissue protein finds extensive application as biocompatible biomaterial in wound healing, as drug carriers, cosmetics, etc. A work has been undertaken to study the stabilization of type I collagen using the plant polyphenol catechin. Catechin treated collagen fibres showed a shrinkage temperature around 70 degrees C implying that catechin is able to impart thermal stability to collagen. Catechin treated collagen fibres has been found to be stable even after treatment with high concentration of the secondary structural destabilizer, urea. Circular dichroism studies revealed that there is no major alteration in the structure of collagen on treatment with catechin. The study has demonstrated the involvement of hydrogen bonding and hydrophobic interactions as the major forces involved in the stabilization of collagen by the plant polyphenol, catechin.
胶原蛋白是一种独特的结缔组织蛋白,作为生物相容性生物材料在伤口愈合、药物载体、化妆品等领域有广泛应用。已开展一项利用植物多酚儿茶素研究I型胶原蛋白稳定性的工作。用儿茶素处理的胶原纤维显示出约70摄氏度的收缩温度,这意味着儿茶素能够赋予胶原蛋白热稳定性。已发现用儿茶素处理的胶原纤维即使在高浓度二级结构去稳定剂尿素处理后仍保持稳定。圆二色性研究表明,用儿茶素处理后胶原蛋白的结构没有重大改变。该研究证明了氢键和疏水相互作用是植物多酚儿茶素稳定胶原蛋白的主要作用力。