title: Proteolytic cleavage reveals interaction patterns between silica nanoparticles and two variants of human carbonic anhydrase.
abstract: To characterize the sites on the protein surface that are involved in the adsorption to silica nanoparticles and the subsequent rearrangements of the protein/nanoparticle interaction, a novel approach has been used. After incubation of protein with silica nanoparticles for 2 or 16 h, the protein was cleaved with trypsin and the peptide fragments were analyzed with mass spectrometry. The nanoparticle surface area was in 16-fold excess over available protein surface to minimize the probability that the initial binding would be affected by other protein molecules. When the fragment patterns obtained in the presence and absence of silica nanoparticles were compared, we were able to characterize the protein fragments that interact with the surface. This approach has allowed us to identify the initial binding sites on the protein structure and the rearrangement of the binding sites that occur upon prolonged incubation with the surface.
authors.affiliation: Divisions of Molecular Biotechnology and Biochemistry, IFM, Linköping University, Sweden.
authors.forename: Martin
authors.initials: M
authors.lastname: Lundqvist
authors.forename: Cecilia
authors.initials: C
authors.lastname: Andresen
authors.forename: Sara
authors.initials: S
authors.lastname: Christensson
authors.forename: Sara
authors.initials: S
authors.lastname: Johansson
authors.forename: Martin
authors.initials: M
authors.lastname: Karlsson
authors.forename: Klas
authors.initials: K
authors.lastname: Broo
authors.forename: Bengt-Harald
authors.initials: BH
authors.lastname: Jonsson
mesh_terms: D000327:Adsorption; D002256:Carbonic Anhydrases; D006801:Humans; D053758:Nanoparticles / Q000737:chemistry; D010446:Peptide Fragments / Q000737:chemistry; D059748:Proteolysis; D012822:Silicon Dioxide / Q000737:chemistry
chemical_list: D010446:Peptide Fragments; D012822:Silicon Dioxide; D002256:Carbonic Anhydrases