Chemical and thermal cross-linking of collagen and elastin hydrolysates.
Chemical and thermal cross-linking of collagen and elastin hydrolysates.
复制标题
胶原蛋白和弹性蛋白水解物的化学交联和热交联。
DOI：
10.1016/j.ijbiomac.2010.08.004
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发表时间：
2010
影响因子：
8.2
通讯作者：
A. Płanecka
中科院分区：
文献类型：
--
作者：
A. Sionkowska;J. Skopińska;M. Gawron;J. Kozłowska;A. Płanecka
研究了可溶于醋酸的胶原蛋白和可溶于水的弹性蛋白水解产物的化学和热交联。胶原蛋白和弹性蛋白水解产物的溶液使用可变浓度的1-乙基-3（3-二甲基氨基丙基）碳二亚胺（EDC）和N-羟基琥珀酰亚胺（NHS）处理。此外，二环氧丙基醚（DEPE）已被用作交联剂。由胶原蛋白和弹性蛋白水解产物制成的膜也用60°C和100°C的温度处理以获得额外的交联。使用FTIR光谱、热分析、AFM和SEM显微镜研究了交联的效果。研究了交联后材料的力学性能和表面性能。结果发现，胶原蛋白和弹性蛋白材料的热和机械性能在热处理后和与EDC/NHS和/或DEPE反应后已经改变。化学交联后的胶原材料的表面性质已被修改。胶原膜的热交联和化学交联导致表面极性的改变。
Chemical and thermal cross-linking of collagen soluble in acetic acid and elastin hydrolysates soluble in water have been studied. Solutions of collagen and elastin hydrolysates were treated using variable concentrations of 1-ethyl-3(3-dimethyl aminopropyl) carbodiimide (EDC) and N-hydroxysuccinimide (NHS). Moreover, diepoxypropylether (DEPE) has been used as cross-linking agent. Films made of collagen and elastin hydrolysates were also treated with temperature at 60°C and 100°C to get additional cross-links. The effect of cross-linking has been studied using FTIR spectroscopy, thermal analysis, AFM and SEM microscopy. Mechanical and surface properties of materials have been studied after cross-linking. It was found that thermal and mechanical properties of collagen and elastin materials have been altered after thermal treatment and after the reactions with EDC/NHS and/or DEPE. Surface properties of collagen materials after chemical cross-linking have been modified. Thermal and chemical cross-linking of collagen films lead to alteration of polarity of the surface.