Lateral Chain Length in Polyalkyl Acrylates Determines the Mobility of Fibronectin at the Cell/Material Interface.
Lateral Chain Length in Polyalkyl Acrylates Determines the Mobility of Fibronectin at the Cell/Material Interface.
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DOI：
10.1021/acs.langmuir.5b03259
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发表时间：
2016-01-26
期刊：
影响因子：
--
通讯作者：
Salmerón-Sánchez M
中科院分区：
文献类型：
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作者：
Bathawab F;Bennett M;Cantini M;Reboud J;Dalby MJ;Salmerón-Sánchez M
细胞通过细胞外基质蛋白层间接与表面相互作用，可以对各种物理性质做出反应，如地形或硬度。聚合物的表面迁移率是另一种不太清楚的物理性质，但已被表明具有调节细胞行为的潜力。聚合物迁移率与系统的玻璃化转变温度（Tg）有关，即聚合物从无定形固体转变为更像液体的状态的点。这项工作表明，聚合物迁移率的变化转化为吸附在材料表面的细胞外基质蛋白的界面迁移率。本研究利用了一个家族的聚烷基丙烯酸酯具有相似的化学性质，但不同程度的迁移，通过增加侧链的长度获得。这些材料与荧光纤维连接蛋白一起用于确定构成初始细胞-物质界面的蛋白质界面层的移动性。此外，还确定了纤维连接蛋白结构域（III9, III10， -整合素结合位点），细胞介导的重组和细胞分化的程度。观察到纤维连接蛋白迁移对聚合物表面迁移的非单调依赖性，在L929成纤维细胞介导的蛋白质层重组中也发现了类似的趋势。整合素结合位点在更灵活的表面上的可用性更高，在这些表面上观察到类似的蛋白质组织在材料界面上形成网络。最后，C2C12成肌细胞的分化在抑制细胞收缩性的情况下对表面流动性高度敏感。总之，这些发现表明，聚合物迁移是一种微妙的影响，通过蛋白质层转化为细胞/材料界面，改变表面的生物活性。
Cells, by interacting with surfaces indirectly through a layer of extracellular matrix proteins, can respond to a variety of physical properties, such as topography or stiffness. Polymer surface mobility is another physical property that is less well understood but has been indicated to hold the potential to modulate cell behavior. Polymer mobility is related to the glass-transition temperature (Tg) of the system, the point at which a polymer transitions from an amorphous solid to a more liquid-like state. This work shows that changes in polymer mobility translate to interfacial mobility of extracellular matrix proteins adsorbed on the material surface. This study has utilized a family of polyalkyl acrylates with similar chemistry but different degrees of mobility, obtained through increasing length of the side chain. These materials are used, in conjunction with fluorescent fibronectin, to determine the mobility of this interfacial layer of protein that constitutes the initial cell–material interface. Furthermore, the extent of fibronectin domain availability (III9, III10, - the integrin binding site), cell-mediated reorganization, and cell differentiation was also determined. A nonmonotonic dependence of fibronectin mobility on polymer surface mobility was observed, with a similar trend noted in cell-mediated reorganization of the protein layer by L929 fibroblasts. The availability of the integrin-binding site was higher on the more mobile surfaces, where a similar organization of the protein into networks at the material interface was observed. Finally, differentiation of C2C12 myoblasts was seen to be highly sensitive to surface mobility upon inhibition of cell contractility. Altogether, these findings show that polymer mobility is a subtle influence that translates to the cell/material interface through the protein layer to alter the biological activity of the surface.