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纳米波纹 TiO2 和 Si 表面的蛋白质吸附。

Protein adsorption on nano-scaled, rippled TiO2 and Si surfaces.

机构信息

Institute of Solid State Physics, Friedrich Schiller University, Jena, Germany.

出版信息

Biointerphases. 2012 Dec;7(1-4):55. doi: 10.1007/s13758-012-0055-5. Epub 2012 Sep 7.

Abstract

We synthesized nano-scaled periodic ripple patterns on silicon and titanium dioxide (TiO(2)) surfaces by xenon ion irradiation, and performed adsorption experiments with human plasma fibrinogen (HPF) on such surfaces as a function of the ripple wavelength. Atomic force microscopy showed the adsorption of HPF in mostly globular conformation on crystalline and amorphous flat Si surfaces as well as on nano-structured Si with long ripple wavelengths. For short ripple wavelengths the proteins seem to adsorb in a stretched formation and align across or along the ripples. In contrast to that, the proteins adsorb in a globular assembly on flat and long-wavelength rippled TiO(2), but no adsorbed proteins could be observed on TiO(2) with short ripple wavelengths due to a decrease of the adsorption energy caused by surface curvature. Consequently, the adsorption behavior of HPF can be tuned on biomedically interesting materials by introducing a nano-sized morphology while not modifying the stoichiometry/chemistry.

摘要

我们通过氙离子辐照在硅和二氧化钛 (TiO(2)) 表面合成了纳米级周期性波纹图案,并研究了波纹波长对人血浆纤维蛋白原 (HPF) 在这些表面上吸附的影响。原子力显微镜显示,HPF 在结晶和平整的 Si 表面以及具有长波纹波长的纳米结构 Si 上以大多呈球形构象吸附。对于短波纹波长,蛋白质似乎以拉伸的形式吸附,并沿或沿波纹排列。与此相反,蛋白质在平整且长波纹波长的 TiO(2)上以球形组装方式吸附,但在短波纹波长的 TiO(2)上由于表面曲率引起的吸附能降低而无法观察到吸附的蛋白质。因此,通过引入纳米级形貌而不改变化学计量/化学性质,可以在生物医学上有趣的材料上调节 HPF 的吸附行为。

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