温度激活的PEG表面分离可控制聚合物的蛋白质排斥性。,Langmuir

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温度激活的PEG表面分离可控制聚合物的蛋白质排斥性。
Langmuir ( IF 3.7 ) Pub Date : 2019-06-30 00:00:00 , DOI: 10.1021/acs.langmuir.9b00702
N Sanjeeva Murthy ₁ , Wenjie Wang ₂ , Sven D Sommerfeld ₁ , David Vaknin ₂ , Joachim Kohn ₂

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聚（乙二醇）（PEG）被广泛用于调节生物材料的水合状态，并经常用于生产不结垢的表面。在这里，我们提供了X射线散射数据，该数据表明PEG的表面偏析，而不仅仅是其在本体中的存在，才通过影响含PEG的底物的亲水性而使之发生。我们展示了一种温度依赖性触发，该触发将含PEG的底物从蛋白质吸附状态转变为蛋白质排斥状态。聚的电影（desaminotyrosyl -酪氨酸合作-PEG碳酸酯）具有较高的PEG含量（20 wt％），预计其中很少的蛋白质吸附，石英晶体微量天平数据显示，在8°C时，纤维蛋白原和牛血清白蛋白的吸附明显。表面在37.5°C时具有蛋白质排斥性。当将相同的聚合物碘化时，即使将37重量％的PEG掺入到聚合物主链中，该聚合物也是蛋白质吸附性的。这表明高的PEG含量本身不足以排斥蛋白质。通过用碘或通过降低温度来抑制相分离，我们表明PEG必须进行相分离并向表面起霜，以形成防污表面。

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Temperature-Activated PEG Surface Segregation Controls the Protein Repellency of Polymers.

Poly(ethylene glycol) (PEG) is widely used to modulate the hydration states of biomaterials and is often applied to produce nonfouling surfaces. Here, we present X-ray scattering data, which show that it is the surface segregation of PEG, not just its presence in the bulk, that makes this happen by influencing the hydrophilicity of PEG-containing substrates. We demonstrate a temperature-dependent trigger that transforms a PEG-containing substrate from a protein-adsorbing to a protein-repelling state. On films of poly(desaminotyrosyl-tyrosine-co-PEG carbonate) with high (20 wt %) PEG content, in which very little protein adsorption is expected, quartz crystal microbalance data showed significant adsorption of fibrinogen and bovine serum albumin at 8 °C. The surface became protein-repellent at 37.5 °C. When the same polymer was iodinated, the polymer was protein-adsorbent, even when 37 wt % PEG was incorporated into the polymer backbone. This demonstrates that high PEG content by itself is not sufficient to repel proteins. By inhibiting phase separation either with iodine or by lowering the temperature, we show that PEG must phase-separate and bloom to the surface to create an antifouling surface. These results suggest an opportunity to design materials with high PEG content that can be switched from a protein-attractant to a protein-repellent state by inducing phase separation through brief exposure to temperatures above their glass transition temperature.

更新日期：2019-06-30

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