Cell adhesion and proliferation on RGD-modified recombinant spider silk proteins
Cell adhesion and proliferation on RGD-modified recombinant spider silk proteins
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DOI：
10.1016/j.biomaterials.2012.05.069
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发表时间：
2012-10-01
期刊：
影响因子：
14
通讯作者：
Scheibel, Thomas
中科院分区：
文献类型：
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作者：
Wohlrab, Stefanie;Mueller, Susanne;Scheibel, Thomas
由于生物相容性和生物降解性以及纤维的机械性能，蜘蛛丝已成为生物医学应用研究人员的一种有吸引力的材料。在这项研究中，工程重组蜘蛛丝蛋白eADF 4（C16）与整合素识别序列RGD通过遗传（融合氨基酸序列GRGDSPG）以及化学方法（使用环肽c（RGDIX））进行修饰。这两种改性的丝蛋白被加工成膜，然后表征有关的二级结构，水接触角和表面粗糙度。可以检测到RGD修饰对任何这些膜性质的影响。然而，贴附和增殖的BALB/3 T3小鼠成纤维细胞上的RGD修饰的丝蛋白制成的薄膜显着改善。有趣的是，遗传产生的杂合蛋白（具有线性RGD序列）显示出与用环状RGD肽化学修饰的丝蛋白相似或略好的细胞粘附特性。(C)2012爱思唯尔有限公司保留所有权利。
Due to the biocompatibility and biodegradability as well as the mechanical properties of the fibers, spider silk has become an attractive material for researchers regarding biomedical applications. In this study, the engineered recombinant spider silk protein eADF4(C16) was modified with the integrin recognition sequence RGD by a genetic (fusing the amino acid sequence GRGDSPG) as well as a chemical approach (using the cyclic peptide c(RGDIX)). Both modified silk proteins were processed into films, and thereafter characterized concerning secondary structure, water contact angle and surface roughness. No influence of the RGD-modifications on any of these film properties could be detected. However, attachment and proliferation of BALB/3T3 mouse fibroblasts were significantly improved on films made of the RGD-modified silk proteins. Interestingly, the genetically created hybrid protein (with a linear RGD sequence) showed similar or slightly better cell adhesion properties as the silk protein chemically modified with the cyclic RGD peptide. (C) 2012 Elsevier Ltd. All rights reserved.