Department of Biomass and Leather Engineering, National Engineering Laboratory for Clean Technology of Leather Manufacture, Sichuan University, Chengdu, Sichuan 610065, China.
Int J Biol Macromol. 2011 Mar 1;48(2):354-9. doi: 10.1016/j.ijbiomac.2010.12.012. Epub 2010 Dec 23.
We have investigated the modification of collagen with a natural plant polyphenol, procyanidin under acidic conditions. Fourier transform infrared spectroscopy (FTIR) and Atomic force microscopy (AFM) studies demonstrate that the hydrogen bond interactions between collagen and procyanidin does not destroy the triple helix conformation of collagen, and the fibril aggregation occurs because of the cross-linking with procyanidin. The water contact angle (WCA) tests indicate that the hydrophobicity of the procyanidin modified collagen films can be improved. Whereas, the water vapor permeability (WVP) of the films decrease with the increasing procyanidin content due to the formation of denser structure. Moreover, differential scanning calorimetry (DSC) and thermogravimetric (TG) measurements reveal that the collagen/procyanidin films have improved thermal stability in comparison with pure collagen. The present study reveals that procyanidin stabilizes collagen as a cross-linker and preserves its triple helical structure.
我们研究了在酸性条件下，天然植物多酚原花青素对胶原蛋白的修饰作用。傅里叶变换红外光谱（FTIR）和原子力显微镜（AFM）研究表明，胶原蛋白与原花青素之间的氢键相互作用不会破坏胶原蛋白的三螺旋构象，而是由于与原花青素的交联导致纤维聚集。水接触角（WCA）测试表明，原花青素修饰的胶原膜的疏水性可以提高。然而，由于形成更致密的结构，随着原花青素含量的增加，膜的水蒸气透过率（WVP）降低。此外，差示扫描量热法（DSC）和热重（TG）测量表明，与纯胶原蛋白相比，胶原蛋白/原花青素膜具有更好的热稳定性。本研究表明，原花青素作为交联剂稳定胶原蛋白并保持其三螺旋结构。
