Surface tailoring for controlled protein adsorption: Effect of topography at the nanometer scale and chemistry
Surface tailoring for controlled protein adsorption: Effect of topography at the nanometer scale and chemistry
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DOI：
10.1021/ja056278e
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发表时间：
2006-03-29
影响因子：
15
通讯作者：
Perry, CC
中科院分区：
文献类型：
--
作者：
Roach, P;Farrar, D;Perry, CC
蛋白质吸附行为是当今许多研究领域的核心，包括生物技术和材料科学。随着对蛋白质-表面相互作用的理解，对固定化物种的构象和取向的控制可能最终允许生成定制的表面。在这方面的贡献，蛋白质表面相互作用已被审查，特别关注表面曲率与表面化学效应。具有亲水性和疏水性表面化学的直径在15-165 nm范围内的二氧化硅球已被用作模型基底。两种不同的蛋白质的大小和形状，牛血清白蛋白（BSA）和牛纤维蛋白原（Fg），已被用于蛋白质结合的模型研究与详细的二级结构分析正在进行使用红外光谱（IR）的表面结合蛋白。虽然两种蛋白质的结合亲和力和饱和值的趋势相似，但白蛋白在较大的基质上越来越不有序，而纤维蛋白原相反，当吸附到具有高表面曲率的颗粒上时，在更大程度上失去二级结构。这些影响通过表面化学复合，两种蛋白质在疏水表面上变得更加变性。表面化学和形貌在确定结合蛋白的结构中起关键作用。这两种蛋白质到具有不同曲率和化学性质的表面上的结合特性的模型。我们建议，吸附的蛋白质层的性质可以通过仔细考虑表面结构，允许制造的材料/表面涂层定制的生物活性的指导。
Protein adsorption behavior is at the heart of many of today's research fields including biotechnology and materials science. With understanding of protein-surface interactions, control over the conformation and orientation of immobilized species may ultimately allow tailor-made surfaces to be generated. In this contribution protein-surface interactions have been examined with particular focus on surface curvature with and without surface chemistry effects. Silica spheres with diameters in the range 15-165 nm with both hydrophilic and hydrophobic surface chemistries have been used as model substrates. Two proteins differing in size and shape, bovine serum albumin (BSA) and bovine fibrinogen (Fg), have been used in model studies of protein binding with detailed secondary structure analysis being performed using infrared spectroscopy (IR) on surface-bound proteins. Although trends in binding affinity and saturation values were similar for both proteins, albumin is increasingly less ordered on larger substrates, while fibrinogen, in contrast, loses secondary structure to a greater extent when adsorbing onto particles with high surface curvature. These effects are compounded by surface chemistry, with both proteins becoming more denatured on hydrophobic surfaces. Both surface chemistry and topography play key roles in determining the structure of the bound proteins. A model of the binding characteristics of these two proteins onto surfaces having differing curvature and chemistry is presented. We propose that properties of an adsorbed protein layer may be guided through careful consideration of surface structure, allowing the fabrication of materials/surface coatings with tailored bioactivity.