期刊
NANO LETTERS
卷 12, 期 3, 页码 1583-1587出版社
AMER CHEMICAL SOC
DOI: 10.1021/nl2044524
关键词
Silica nanoparticles; chemical modification; quantitative proteomics; protein orientation
类别
资金
- Nanoscale Science and Engineering Initiative of the National Science Foundation [DMR-0642573]
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..
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