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首页> 外文期刊>Langmuir: The ACS Journal of Surfaces and Colloids >Self-assembly process of soft ferritin-PNIPAAm conjugate bionanoparticles at polar-apolar interfaces
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Self-assembly process of soft ferritin-PNIPAAm conjugate bionanoparticles at polar-apolar interfaces

机译:软铁蛋白-PNIPAAm共轭纳米粒子在极性-非极性界面的自组装过程

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摘要

We describe an in-depth investigation on the dynamics and assembly behavior at polar-apolar interfaces of ferritin-PNIPAAm conjugates (poly-N- isopropylacrylamide). The stabilization of oil-water interfaces by the modified ferritin was investigated by dynamic surface tension measurements and compared to the individual components of the bionanoparticle conjugate, namely, unmodified ferritin and pure PNIMAAm of similar molecular weight. It was found that the modified ferritin, even at a low particle concentration, rapidly reduces the interfacial tension. The difference in interfacial stabilization was also shown by cryo-scanning electron microscopy and scanning force microscopy, which displayed very different morphologies at the polar-apolar interface for the unmodified ferritin, pure PNIPAAm, and the ferritin-PNIPAAm conjugate, respectively. The self-assembly of the ferritin-PNIPAAm was further analyzed by cryo-transmission electron microscopy and fluorescence microscopy, for which a fluorescently labeled polymer was used. Both techniques revealed details on the assembly of the protein-polymer conjugate at the oil-water interface.
机译:我们描述了对铁蛋白-PNIPAAm共轭物(聚-N-异丙基丙烯酰胺)的极性-非极性界面的动力学和组装行为的深入研究。通过动态表面张力测量研究了改性铁蛋白对油水界面的稳定作用,并将其与生物纳米粒子共轭物的各个成分进行了比较,即未改性铁蛋白和分子量相似的纯PNIMAAm。发现即使在低颗粒浓度下,改性铁蛋白也迅速降低了界面张力。冷冻扫描电子显微镜和扫描力显微镜也显示了界面稳定性的差异,它们分别在未修饰的铁蛋白,纯PNIPAAm和铁蛋白-PNIPAAm共轭物的极性-非极性界面上显示出非常不同的形态。铁蛋白-PNIPAAm的自组装通过冷冻透射电子显微镜和荧光显微镜进一步分析,为此使用了荧光标记的聚合物。两种技术都揭示了蛋白质-聚合物结合物在油-水界面处的组装细节。

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