Abstract

Fibroin is a protein that has been extensively studied for biomedical application. In the present study, silk was dissolved in CaCl₂-C₂H₅OH-H₂O in order to obtain silk fibroin (SF) solution, and it was then lyophilized in freeze-dryer. The electrospinning of SF sponge was performed at different fibroin concentrations. SF nanofibers were modified by crosslinking PAMAM dendrimers to carboxylic-terminated fibroin, via EDC and NHS. The modified SF nanofibers scaffold was evaluated by SEM, X-Ray diffraction, FTIR and MTT assay. SEM micrograph showed that the electrospun containing 7% (w/w) fibroin had continuous fibers and an average diameter of 80 nm. Through treatment, conformational transitions of the SF nanofibers from random coil to β-sheet occurred rapidly, confirmed by FTIR and X-Ray diffraction. FTIR spectrum showed amide peaks, which confirmed the existence of fibroin. The modification results of analysis demonstrated that the amino groups were more established on the surface of the SF nanofiber scaffold. Biocompatibility tests were carried out through seeding fibroblasts cell line L929 on nanofibers. Adhesion and proliferation of fibroblasts were investigated by MTT assay, which showed no cytotoxicity. Therefore, fibroin nanofibers scaffolds appear to be a probable choice for potential use in tissue engineering.

摘要

丝心蛋白是已经广泛研究用于生物医学应用的蛋白质。在本研究中，将丝溶解在CaCl ₂ -C ₂ H ₅ OH-H ₂ O中以获得丝素蛋白（SF）溶液，然后将其在冷冻干燥机中冻干。SF海绵的静电纺丝是在不同的纤维蛋白浓度下进行的。SF纳米纤维通过交联PAMAM树状与羧酸封端的丝心蛋白修饰，通过EDC和NHS。通过SEM，X射线衍射，FTIR和MTT分析评价了改性SF纳米纤维支架。SEM显微照片表明，含有7％（w / w）纤维蛋白的电纺丝具有连续纤维，平均直径为80nm。通过FTIR和X射线衍射证实，通过处理，SF纳米纤维从无规卷曲迅速转变为β-折叠的构象转变。FTIR光谱显示酰胺峰，这证实了纤维蛋白的存在。分析的修饰结果表明，氨基在SF纳米纤维支架的表面上更牢固。通过将成纤维细胞细胞株L929接种在纳米纤维上进行生物相容性测试。MTT法检测成纤维细胞的黏附和增殖，未见细胞毒性。因此，