Functionalised amyloid fibrils for roles in cell adhesion
Functionalised amyloid fibrils for roles in cell adhesion
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DOI：
10.1016/j.biomaterials.2007.11.028
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发表时间：
2008-04-01
期刊：
影响因子：
14
通讯作者：
MacPhee, Cait E.
中科院分区：
文献类型：
--
作者：
Gras, Sally L.;Tickler, Anna K.;MacPhee, Cait E.
我们描述了旨在探索使用淀粉样原纤维作为新型纳米级生物材料来促进和利用体外细胞粘附、迁移和分化的可能性的实验。我们创建了将生物细胞粘附序列 (RGD) 或控制序列 (RAD) 添加到与淀粉样蛋白转甲状腺素蛋白的残基 105-115 相对应的 11 残基肽的 C 末端的肽。这些肽很容易在水溶液中自组装形成淀粉样蛋白原纤维，X射线纤维衍射表明它们在特征性交叉β结构中具有与母体肽形成的原纤维相同的链和片层间距。我们报告说，含有 RGD 序列的原纤维具有生物活性，并且这些原纤维通过原纤维表面上显示的 RGD 基团与细胞发生特异性相互作用。由于这种功能化原纤维的设计可以系统地改变，这些发现表明，有可能生成基于淀粉样原纤维的纳米材料，这些纳米材料经过定制以促进与多种细胞类型的相互作用。 (c) 2007 Elsevier Ltd. 保留所有权利。
We describe experiments designed to explore the possibility of using amyloid fibrils as new nanoscale biomaterials for promoting and exploiting cell adhesion, migration and differentiation in vitro. We created peptides that add the biological cell adhesion sequence (RGD) or a control sequence (RAD) to the C-terminus of an 11-residue peptide corresponding to residues 105-115 of the amyloidogenic protein transthyretin. These peptides readily self-assemble in aqueous solution to form amyloid fibrils, and X-ray fibre diffraction shows that they possess the same strand and sheet spacing in the characteristic cross-beta structure as do fibrils formed by the parent peptide. We report that the fibrils containing the RGD sequence are bioactive and that these fibrils interact specifically with cells via the RGD group displayed on the fibril surface. As the design of such functionalized fibrils can be systematically altered, these findings suggest that it will be possible to generate nanomaterials based on amyloid fibrils that are tailored to promote interactions with a wide variety of cell types. (c) 2007 Elsevier Ltd. All rights reserved.