Stabilization of collagen with EDC/NHS in the presence of L-lysine: a comprehensive study.
Stabilization of collagen with EDC/NHS in the presence of L-lysine: a comprehensive study.
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DOI：
10.1016/j.colsurfb.2011.10.002
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发表时间：
2012-02
期刊：
影响因子：
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通讯作者：
R. Usha;K. J. Sreeram;A. Rajaram
中科院分区：
文献类型：
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作者：
R. Usha;K. J. Sreeram;A. Rajaram
本文报道了L-赖氨酸对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)交联胶原的构象、流变学和热性能的影响，并研究了L-赖氨酸对胶原自组装过程的影响。在没有 L-赖氨酸的情况下，与 EDC/NHS 交联的胶原蛋白的流变学特征显示，剪切应力随着剪切速度的增加而增加，表明胶原蛋白链变得刚性并且分子难以流动。另一方面，在存在 L-赖氨酸的情况下，剪切应力随剪切速度的增加相对较小，这表明胶原蛋白分子具有更大的柔韧性。使用粉末 XRD、FT-IR、偏光光学显微镜和动力学研究来表征在不存在和存在 L-赖氨酸的情况下经 EDC/NHS 处理的胶原蛋白的自组装过程。 XRD 研究表明，L-赖氨酸存在时峰强度和锐度增加，表明胶原纳米原纤维的结晶度增强。 FT-IR 结果表明，EDC/NHS 交联中 L-赖氨酸的掺入有利于胶原蛋白的分子稳定性。从本研究中可以得出结论，用 L-赖氨酸预处理胶原蛋白可增强 EDC/NHS 交联，可用于生物材料应用。
This paper reports the effect of l-lysine on the conformational, rheological, and thermal properties of 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide (EDC) and N-hydroxysuccinimide (NHS) cross linked collagen and investigates the influence of l-lysine on the self assembly processes of collagen. In the absence of l-lysine, the rheological characterization of collagen cross linked with EDC/NHS showed an increase in shearing stress with shearing speed indicating that the collagen chains become rigid and the molecules are reluctant to flow. On the other hand, the increase in shearing stress with shearing speed is comparatively much less in the presence of l-lysine indicating a greater flexibility of the collagen molecules. The self assembly processes of collagen treated with EDC/NHS in the absence and presence of l-lysine were characterized using powder XRD, FT-IR, polarizing optical microscopy and kinetic studies. XRD studies show an increase in peak intensity and sharpness in the presence of l-lysine indicating the enhancement of crystallinity of collagen nano-fibrils. FT-IR results suggest that the incorporation of l-lysine in the EDC/NHS cross linking favors the molecular stability of collagen. From the present study, it is possible to conclude that the pre-treatment of collagen with l-lysine enhances EDC/NHS cross linking and can be used for biomaterial applications.