Department of Biomedical Engineering, 149 Weill Hall, Cornell University, Ithaca, New York 14853, USA.
J Biomed Mater Res A. 2010 Jun 1;93(3):843-51. doi: 10.1002/jbm.a.32231.
This study focuses on the development of a novel method of nonenzymatic glycation of fibrillar collagen gels. In contrast to previous studies in which type I collagen gels were glycated in the solid state, this study presents a method for glycation in solution. The type I collagen in solution or gels was exposed to a range of ribose concentrations from 0 to 250 mM. The binding of ribose to collagen was documented using Fourier transform infrared (FTIR) spectroscopy. formation of advanced glycation end products (AGEs) was quantified by fluorescence measurement. The bulk compressive modulus and viscoelastic time constant of processed gels were determined in stress relaxation studies. Both methods of glycation enhanced ribose addition and AGE formation in a dose-dependent manner, with glycation in the gel state being more efficient. Both methods enhanced mechanical properties similarly, with 250 mM ribose treatment resulting in a 10-fold increase in bulk modulus.
本研究专注于开发一种新型纤维胶原蛋白凝胶非酶糖化方法。与之前将 I 型胶原蛋白凝胶在固态下糖化的研究不同，本研究提出了一种在溶液中糖化的方法。将溶液或凝胶中的 I 型胶原蛋白暴露于 0 至 250mM 的一系列核糖浓度下。使用傅里叶变换红外（FTIR）光谱记录核糖与胶原蛋白的结合情况。通过荧光测量定量测定晚期糖基化终产物（AGEs）的形成。在应力松弛研究中，确定处理后凝胶的体压缩模量和粘弹时变常数。两种糖化方法均以剂量依赖的方式增强了核糖的添加和 AGE 的形成，而凝胶状态下的糖化效率更高。两种方法同样增强了机械性能，250mM 核糖处理使体模量增加了 10 倍。
