Fabrication of Gold Nanoparticles Inside Unmodified Horse Spleen Apoferritin

Abstract

Size‐constrained gold nanoparticles are successfully synthesized within the cavity of native horse spleen ferritin by using a two‐step process relying on the initial formation of nanoclusters. The particles co‐elute with the nanocage ferritin by chromatography, indicating that the particles are associated with intact protein cages. Further characterization reveals that the growth of the monodisperse particles is limited by the protein cage.

Rational disruption of the oligomerization of the mini‐ferritin E. coli DPS through protein‐protein interface mutation

“…1,2 Moreover, protein-protein interactions are also integral to the generation of cellular selfassembled nano-structures, and establishing how they control self-assembly could lead not only to fundamental understanding but also to the eventual rational design of novel structures for a myriad of applications such as the templation of inorganic nano-materials and for encapsulated reaction chemistry. [3][4][5][6][7][8] Although protein-protein interactions are intriguing medicinal targets, they have only recently been pursued for drug development studies somewhat owing to the discovery that although they often involve large, buried surface area, they can be inhibited using low molecular weight small molecules that target ''hot spot'' residues where the binding energy is concentrated. 9,10 Alanine shaving, where individual side changes are conceptually shaved to a methyl residuum and where the stabilities of the resulting mutants are determined with respect to wild type, is the most common method to identify hot spot residues.…”

Biomolecular Imaging at High Spatial and Temporal Resolution In Vitro and In Vivo

“…Notably, ferritin has shown use as a tag for soluble intracellular proteins that is visible by TEM after incubation with iron compounds [57]. It may be that mutating ferritin to bind other, more electron dense, substrates could improve the tag [60,61]. Alternatively, cadmium selenide (CdSe) can be mineralised within the ferritin cage [62].…”

“…Therefore, low defocus (high resolution but low contrast) images can be taken prior to high defocus (low resolution but high contrast) images. The particles are then identified in the second image before their positions are used to extract the data from the high-resolution first image [60]. Reconstructing 3D models of proteins is the obvious successor to 2D views.…”

Use of the confined spaces of apo-ferritin and virus capsids as nanoreactors for catalytic reactions

“…The threefold channels used to transfer ions into and out of the protein. These properties make ferritin an important platform for preparing nanomaterials, and for use in drug delivery and catalysis [22][23][24][25][26][27]. For example, the ferritin cage can encapsulate Gd-HPDO3A (gadolinium-[10-(2-hydroxypropyl)-1,4,7,10-tetraazacyclododecane-1,4,7-triacetic acid]) chelates via a reassembly/disassembly mechanism and exhibits 20 times higher relaxivity compared to the free Gd-HPDO3A chelate in water [23].…”