Rensselaer Nanotechnology Center, Rensselaer Polytechnic Institute, Troy, New York 12180, USA.
Nano Lett. 2012 Mar 14;12(3):1583-7. doi: 10.1021/nl2044524. Epub 2012 Feb 9.
We describe a method for determining the orientation of cytochrome c, RNase A, and lysozyme on silica nanoparticles (SNPs) using chemical modification combined with proteolysis-mass spectrometry. The proteins interacted with SNPs through preferential adsorption sites, which are dependent on SNP diameter; 4 nm SNPs induce greater structural stabilization than 15 nm particles, presumably due to greater surface curvature of the former. These results suggest that nanoparticle size and protein structure influence protein orientation on SNPs.
我们描述了一种使用化学修饰结合蛋白水解质谱法来确定细胞色素 c、核糖核酸酶 A 和溶菌酶在二氧化硅纳米颗粒（SNPs）上取向的方法。这些蛋白质通过优先吸附位点与 SNPs 相互作用，这些吸附位点取决于 SNP 的直径；4nm 的 SNPs 比 15nm 的颗粒诱导更大的结构稳定性，这可能是由于前者具有更大的表面曲率。这些结果表明，纳米颗粒的大小和蛋白质的结构影响蛋白质在 SNPs 上的取向。
