Protein adsorption on model surfaces with controlled nanotopography and chemistry
Protein adsorption on model surfaces with controlled nanotopography and chemistry
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DOI：
10.1021/la011011o
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发表时间：
2002-02-05
期刊：
影响因子：
3.9
通讯作者：
Dufrêne, YF
中科院分区：
文献类型：
--
作者：
Denis, FA;Hanarp, P;Dufrêne, YF
为了评估蛋白质吸附过程中的基质表面特性的影响，我们研究了胶原蛋白的吸附（吸附量，超分子组织）模型基质表现出控制的地形和表面化学。基质分两步制备：（i）将金沉积到硅晶片（光滑基质）和通过胶体光刻法产生的具有纳米级突起的支撑物（粗糙基质）上;（ii）使用烷基乙醇自组装，用CH 3（疏水）和OH（亲水）基团进行官能化。原子力显微镜（AFM）图像记录在水中，胶原蛋白吸附之前和之后，并使用两种独立的方法对图像进行定量分析。在光滑的基质上，胶原蛋白在亲水性表面上形成了一个大约6 nm厚的均匀层，具有低粗糙度，在疏水性表面上形成了一个大约20 nm厚的层，显示出细长的聚集结构。薄膜厚度测量（AFM）与X-射线光电子能谱（XPS）显示更大的吸附量相比，亲水性的疏水表面。在粗糙的基质上，吸附量与光滑基质上的吸附量相似;然而，胶原分子不再在疏水表面上形成聚集结构。它的结论是，而吸附量只受表面化学，吸附层的超分子组织控制的表面化学和地形。这里提出的方法将有很大的价值，在生物物理学研究的生物吸附和生物粘附过程的定义的表面特性的基质。
To evaluate the influence of substratum surface characteristics on protein adsorption processes, we have investigated the adsorption (adsorbed amount, supramolecular organization) of collagen on model substrata exhibiting controlled topography and surface chemistry. Substrata were prepared in two steps: (i) gold deposition onto silicon wafers (smooth substrata) and onto a support with nanoscale protrusions created by colloidal lithography (rough substrata); (ii) functionalization with CH3 (hydrophobic) and OH (hydrophilic) groups, using alkanethiol self-assembly. Atomic force microscopy (AFM) images were recorded under water, prior to and after collagen adsorption, and the images were analyzed quantitatively using two independent approaches. On smooth substrata, collagen formed a similar to6 nm thick, homogeneous layer with low roughness on hydrophilic surfaces, and a similar to20 nm thick layer exhibiting elongated aggregated structures on hydrophobic surfaces. Film thickness measurements (AFM) together with X-ray photoelectron spectroscopy (XPS) revealed larger adsorbed amounts on hydrophobic surfaces compared to hydrophilic ones. On rough substrata, the adsorbed amounts were similar to those found on smooth substrata; however, the collagen molecules no longer formed aggregated structures on the hydrophobic surfaces. It is concluded that while the adsorbed amount is only affected by the surface chemistry, the supramolecular organization of the adsorbed layer is controlled both by surface chemistry and topography. The approach presented here will have great value in biophysics for investigating bioadsorption and bioadhesion processes on substrata of defined surface properties.