title: Position-specific chemical modification and quantitative proteomics disclose protein orientation adsorbed on silica nanoparticles.
abstract: 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.
authors.affiliation: Rensselaer Nanotechnology Center, Rensselaer Polytechnic Institute, Troy, New York 12180, USA.
authors.forename: Siddhartha
authors.initials: S
authors.lastname: Shrivastava
authors.forename: Joseph H
authors.initials: JH
authors.lastname: Nuffer
authors.forename: Richard W
authors.initials: RW
authors.lastname: Siegel
authors.forename: Jonathan S
authors.initials: JS
authors.lastname: Dordick
mesh_terms: D000327:Adsorption; D001665:Binding Sites; D013058:Mass Spectrometry; D008422:Materials Testing; D049329:Nanostructures / Q000737:chemistry* / Q000648:ultrastructure; D011485:Protein Binding; D025941:Protein Interaction Mapping / Q000379:methods*; D011506:Proteins / Q000737:chemistry*; D012822:Silicon Dioxide / Q000737:chemistry*; D013499:Surface Properties
chemical_list: D011506:Proteins; D012822:Silicon Dioxide