丁二酰化对胶原生物活性结构的影响

本实验以猪皮胶原为研究对象,通过丁二酸酐改性制备了酰化胶原,采用仪器分析法对酰化胶原三股螺旋结构的保留程度进行检测,在此基础上使用原子力显微镜和成纤维细胞培养实验对酰化胶原的生物活性进行了进一步考察。结果表明:胶原的酰化度为62.4%,酰化胶原的等电点降低到4.1。X射线衍射(X-ray diffraction,XRD)、热变性温度、圆二色谱法检测结果显示,丁二酸酐改性整体上并未破坏胶原的三股螺旋结构;酰化胶原在原子力显微镜下呈现了胶原特有的纤维结构,成纤细胞培养实验结果发现酰化胶原可以兼容成纤细胞,并在一定程度上促进成纤细胞的增殖,丁二酰化不会破坏胶原的生物活性结构。

Effect of Acetylation on Biological Activity and Structure of Collagen

In this study, acylated collagen from pig skin was prepared by succinic anhydride modification. The degree of
retention of the collagen triple helix structure was detected by instrumental analysis, and then the biological activity of
acylated collagen was further investigated through atomic force microscopy and fibroblast culture. The results showed that
the acylation degree of collagen was 62.4%, and the isoelectric point of acylated collagen decreased to 4.1. X-Ray diffraction
(XRD) analysis, thermal denaturation temperature determination, and circular dichroism analysis indicated that the triple
helix structure of collagen was not destroyed after modification by succinic anhydride. The acetylated collagen presented
specific fiber structure under atomic force microscope. Fibroblast culture experiments showed the acetylated collagen could
be compatible with fibroblast cells, and partly promote their proliferation. To conclude, acetylation does not destroy the
biological activity and structure of collagen.