title: Identifying specific protein residues that guide surface interactions and orientation on silica nanoparticles.
abstract: We identify specific acylphosphatase (AcP) residues that interact with silica nanoparticles (SNPs) using a combined NMR spectroscopy and proteomics-mass spectrometry approach. AcP associated with 4- and 15-nm diameter SNPs through a common and specific interaction surface formed by amino acids from the two α-helices of the protein. Greater retention of native protein structure was obtained on 4-nm SNPs than on 15-nm particles, presumably due to greater surface curvature-induced protein stabilization with the smaller SNPs. These results demonstrate that proteins may undergo specific and size-dependent orientation on nanoparticle surfaces. Our approach can be broadly applied to various protein-material systems to help understand in much greater detail the protein-nanomaterial interface; it would also encourage better modeling, and thus prediction and design, of the behavior of functional proteins adsorbed onto different surfaces.
authors.affiliation: Rensselaer Nanotechnology Center, Rensselaer Polytechnic Institute, Troy, New York 12180, United States.
authors.forename: Siddhartha
authors.initials: S
authors.lastname: Shrivastava
authors.forename: Scott A
authors.initials: SA
authors.lastname: McCallum
authors.forename: Joseph H
authors.initials: JH
authors.lastname: Nuffer
authors.forename: Xi
authors.initials: X
authors.lastname: Qian
authors.forename: Richard W
authors.initials: RW
authors.lastname: Siegel
authors.forename: Jonathan S
authors.initials: JS
authors.lastname: Dordick
mesh_terms: D053758:Nanoparticles / Q000737:chemistry*; D011506:Proteins / Q000737:chemistry*; D012822:Silicon Dioxide / Q000737:chemistry*; D013499:Surface Properties
chemical_list: D011506:Proteins; D012822:Silicon Dioxide