title: Efficient self-assembly of Archaeoglobus fulgidus ferritin around metallic cores.
abstract: Interfacing biological systems with inorganic nanoparticles is of great interest, as it offers means of particle stabilization and spatial control in electronic or biomedical applications. We report on the particle-directed assembly of hyperthermophile Archaeoglobus fulgidus ferritin subunits around negatively charged colloidal gold. An annealing process allows rapid assembly of the protein in near-native stoichiometry. Transmission electron microscopy suggests that greater than 95% of nanoparticles are encapsulated while the self-assembly process ensures that almost 100% of the assembled ferritin cavities are occupied.
authors.affiliation: Department of Chemistry, University of Pennsylvania, 231 South 34th Street, Philadelphia, Pennsylvania 19104-6323, USA.
authors.forename: Joe
authors.initials: J
authors.lastname: Swift
authors.forename: Christopher A
authors.initials: CA
authors.lastname: Butts
authors.forename: Jasmina
authors.initials: J
authors.lastname: Cheung-Lau
authors.forename: Vijay
authors.initials: V
authors.lastname: Yerubandi
authors.forename: Ivan J
authors.initials: IJ
authors.lastname: Dmochowski
mesh_terms: D019611:Archaeoglobus fulgidus / Q000737:chemistry* / Q000648:ultrastructure; D005293:Ferritins / Q000737:chemistry* / Q000378:metabolism; D053768:Metal Nanoparticles / Q000737:chemistry* / Q000648:ultrastructure; D046529:Microscopy, Electron, Transmission; D008958:Models, Molecular; D055503:Protein Multimerization; D017434:Protein Structure, Tertiary; D021122:Protein Subunits / Q000737:chemistry / Q000378:metabolism; D013499:Surface Properties
chemical_list: D021122:Protein Subunits; D005293:Ferritins