Efficient self-assembly of Archaeoglobus fulgidus ferritin around metallic cores.
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.
Swift
Joe
J
Department of Chemistry, University of Pennsylvania, 231 South 34th Street, Philadelphia, Pennsylvania 19104-6323, USA.
Butts
Christopher A
CA
Cheung-Lau
Jasmina
J
Yerubandi
Vijay
V
Dmochowski
Ivan J
IJ
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
D021122:Protein Subunits; D005293:Ferritins