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用天然衍生的交联剂海藻酸钠二醛修饰胶原蛋白。

Modification of collagen with a natural derived cross-linker, alginate dialdehyde.

机构信息

Department of Biomass Chemistry and Engineering, Sichuan University, Chengdu, Sichuan 610065, China; Research Center of Biomedical Engineering, Sichuan University, Chengdu, Sichuan 610065, China.

College of Polymer Science and Engineering, Sichuan University, Chengdu, Sichuan 610065, China.

出版信息

Carbohydr Polym. 2014 Feb 15;102:324-32. doi: 10.1016/j.carbpol.2013.11.050. Epub 2013 Dec 4.

DOI:10.1016/j.carbpol.2013.11.050
PMID:24507288
Abstract

The interaction between collagen and a natural derived cross-linker alginate dialdehyde (ADA) was investigated. Fourier transform infrared (FTIR) spectroscopy and the circular dichroism (CD) measurements indicate that the structure integrity of collagen is still maintained after the ADA treatment, while the differential scanning calorimetry (DSC) study suggests that ADA could promote collagen-ADA membrane's thermostability compared to pure collagen. And the atomic force microscopy (AFM) of cross-linked collagen reveals a denser network structure. Besides, the water contact angle test indicates that the hydrophilic property of collagen-ADA membrane is promoted, which is favorable for cell's attachment and proliferation. Meanwhile, the cytocompatibility results imply that not only no extra cytotoxicity is introduced into the collagen-ADA membrane after ADA treatment, but also collagen-ADA membrane facilitates cell's proliferation when the content of ADA is less than 20%. In conclusion, our study reveals that ADA stabilizes collagen as a cross-linker and preserves its triple helical structure.

摘要

研究了胶原蛋白与天然衍生的交联剂藻酸盐二醛(ADA)之间的相互作用。傅里叶变换红外(FTIR)光谱和圆二色性(CD)测量表明,ADA 处理后胶原蛋白的结构完整性得以保持,而差示扫描量热法(DSC)研究表明,与纯胶原蛋白相比,ADA 可以提高胶原蛋白-ADA 膜的热稳定性。交联胶原蛋白的原子力显微镜(AFM)显示出更密集的网络结构。此外,水接触角测试表明,胶原蛋白-ADA 膜的亲水性得到了提高,有利于细胞的附着和增殖。同时,细胞相容性结果表明,ADA 处理后胶原蛋白-ADA 膜不仅没有引入额外的细胞毒性,而且当 ADA 含量小于 20%时,胶原蛋白-ADA 膜还促进细胞增殖。综上所述,我们的研究表明,ADA 作为交联剂稳定了胶原蛋白并保留了其三螺旋结构。

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