Denatured thiolated collagen .2. Cross-linking by oxidation
Denatured thiolated collagen .2. Cross-linking by oxidation
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DOI：
10.1016/s0142-9612(97)00003-3
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发表时间：
1997-06-01
期刊：
影响因子：
14
通讯作者：
Gagnieu, CH
中科院分区：
文献类型：
--
作者：
Nicolas, FL;Gagnieu, CH
我们最近描述了一种用于变性胶原蛋白硫醇化的新方法，该方法可以将精确数量的 SH 基团附着到蛋白质主链上。变性的硫醇化胶原蛋白的氧化产生二硫化物交联。这些产品的交联经过研究、优化，并与天然和变性胶原蛋白与 0.5% 戊二醛水溶液的交联进行了比较。制备了薄膜，并评估了其拉伸机械性能以及胰蛋白酶和胶原酶的生物降解率。我们的结果表明，氧化硫醇化胶原蛋白中的交联取决于形成的二硫桥的数量及其分子间与分子内的重新分配。由于二硫键的数量可以通过变性胶原蛋白中硫醇的水平和氧化过程来控制，因此可以控制这些新材料的机械性能和生物降解速率。在优化条件下，氧化变性硫醇化胶原蛋白膜比戊二醛交联胶原蛋白膜更具抵抗力和刚性。交联的硫醇化胶原材料也更能抵抗胶原酶降解。然而，由于三螺旋结构的丧失，相对于戊二醛交联的三螺旋胶原蛋白，它们更容易被胰蛋白酶降解。通过二硫桥等生理桥交联的变性胶原蛋白具有可控的机械性能和生物降解速率，具有相当有趣的生物医学应用。 (C) 1997 爱思唯尔科学有限公司。
We have recently described a new method for the thiolation of denatured collagen, which allows precise amounts of SH groups to be attached onto the protein backbone. The oxidation of denatured thiolated collagen produces disulphide cross-linking. The cross-linking of these products has been studied, optimized and compared to the cross-linking of native and denatured collagen with 0.5% aqueous glutaraldehyde. Films have been prepared and their tensile mechanical properties and biodegradation rates with trypsin and collagenase have been evaluated. Our results indicate that the cross-linking in oxidized thiolated collagen depends on the number of the disulphide bridges formed and on their intermolecular versus intramolecular repartition. Since the number of disulphide bridges can be controlled by the level of thiol in the denatured collagen and by the oxidation procedure, it is possible to control the mechanical properties and the biodegradation rates of these new materials. Under optimized conditions, oxidized denatured thiolated collagen films are more resistant and rigid than glutaraldehyde-cross-linked collagen films. Cross-linked thiolated collagen materials are also more resistant to collagenase degradation. However, because of the loss of the triple-helical structure, they are more susceptible to trypsin degradation relative to glutaraldehyde-cross-linked triple-helical collagen. Denatured collagen cross-linked by physiological bridges such as disulphide bridges, with controllable mechanical properties and biodegradation rates, is of considerable interesting biomedical applications. (C) 1997 Elsevier Science Limited.