Dissolution and regeneration of non-mulberry Eriogyna Pyretorum silk fibroin
Dissolution and regeneration of non-mulberry Eriogyna Pyretorum silk fibroin
复制标题
非桑枇杷丝素蛋白的溶解与再生
DOI：
10.1088/2053-1591/aa8e07
复制
发表时间：
2017
影响因子：
2.3
通讯作者：
You Renchuan
中科院分区：
文献类型：
--
作者：
Guo Yuhang;Li Xiufang;Zhang Qiang;Yan Shuqin;You Renchuan
蛋白质基材料因其无毒、生物相容性和生物可降解性而成为生物材料的研究热点。在这项工作中，我们证明了Eriogyna pyvanum丝素蛋白（ESF），一种非桑蚕丝蛋白，作为生物材料的潜力。用Ca（NO3）2/H2O/C2 H5 OH溶液可使脱胶后的ESF纤维完全溶解，生成再生ESF。溶解度强烈依赖于C2 H5 OH的加入量、加热温度和溶解时间。ESF水溶液中的分子构象主要为α-螺旋和无规卷曲。研究了再生ESF的溶胶-凝胶转变行为，表明再生ESF在凝胶化过程中发生了由无规卷曲/α-螺旋向β-折叠的构象转变。特别是，ESF显示出比桑葚丝素蛋白（BSF）更快的凝胶化。因此，BSF的凝胶化速率可以通过改变ESF的比例控制在几十分钟到几天的范围内，为丝水凝胶的制备提供了有用的选择。用乙醇水溶液诱导结构转变，可获得水稳定的再生ESF膜。拉伸测试表明，ESF膜具有约31.0MPa的干强度和约3.3MPa的湿强度。这项研究为生物医学应用提供了替代天然蛋白质材料的新机会。
Protein-based materials have been actively pursued as biomaterials because of their nontoxicity, biocompatibility and biodegradability. In this work, we demonstrated the potential of Eriogyna pyretorum silk fibroin (ESF), a non-mulberry silk protein, as biomaterials. The degummed ESF fibers could be dissolved completely by Ca(NO3)2/H2O/C2H5OH solution to produce regenerated ESF. The solubility was strongly dependent on the addition of C2H5OH, heating temperature and dissolving time. α-helix and random coil are main molecular conformation in aqueous ESF solution. The sol–gel transition behavior of regenerated ESF was also studied, indicating that the conformational transition of regenerated ESF from random coil/α-helix to β-sheet during gelation. Especially, ESF showed more rapid gelation than mulberry silk fibroin (BSF). Consequently, the gelation rate of BSF could be controlled ranging from tens of minutes to days by changing the ESF ratio, providing useful options for the fabrication of silk hydrogels. Water-stable regenerated ESF film could be achieved by using aqueous ethanol to induce structural transition. Tensile tests showed that the ESF films have a dry strength of approximate 31.0 MPa and a wet strength of approximate 3.3 MPa. This study provides new opportunities as an alternative natural protein material for biomedical applications.