Structural characterization of magnetoferritin

Physico-chemical characterization of biomacromolecule magnet of erritin in terms of morphology, structural and magnetic properties shows that iron oxides can be efficiently loaded into apoferritin molecules, preserving its native, bio-compatible structure. At the same time, such loading affects the morphology of the protein shell

Synthesis and Characterization of Magnetoferritin

The paper presents detailed experimental study of synthesis and characterization a bioinorganic magnetic molecule - magnetoferritin. Magnetoferritin with loading of iron ions per protein molecule in the range from 300 to 3000 was prepared. Size distribution analysis (transmission electron microscopy, dynamic light scattering) shows spherical nanoparticles with particle size distribution from 2 to 12 nm, and hydrodynamic diameter from 12 to 25 nm. The thermomagnetic curves measured after cooling the sample in zero field (zero-field cooling) and under the presence of the measurement field (field cooling) show superparamagnetic behavior with the blocking temperature $T_{b}$ from 22 to 60 K and the magnetization loops measured below $T_{b}$ (at 2 K) show the hysteresis with coercive field from 20 to 30 kA/m depending on the concentration of the magnetic nanoparticles

Magnetic Birefringence Study of the Magnetic Core Structure of Ferritin

Magnetically induced optical birefringence (Δ n) was measured for magnetoferritin and horse spleen ferritin aqueous suspensions. The Δ n for magnetoferritin was described in the frame of the Langevin formalism taking into account distribution of core diameter. The established average magnetic dipole moment and core diameter is equal to about 460 $μ_{B}$ and 3 nm, respectively. It was shown that magnetic birefringence and the Cotton-Mouton constant can be powerful parameters in identification of the magnetic core structure of ferritin, especially useful in biomedicine

Effect of iron oxide loading on magnetoferritin structure in solution as revealed by SAXS and SANS

Synthetic biological macromolecule of magnetoferritin containing an iron oxide core inside a protein shell (apoferritin) is prepared with different content of iron. Its structure in aqueous solution is analysed by small-angle synchrotron X-ray (SAXS) and neutron (SANS) scattering. The loading factor (LF) defined as the average number of iron atoms per protein is varied up to LF = 800. With an increase of the LF, the scattering curves exhibit a relative increase in the total scattered intensity, a partial smearing and a shift of the match point in the SANS contrast variation data. The analysis shows an increase in the polydispersity of the proteins and a corresponding effective increase in the relative content of magnetic material against the protein moiety of the shell with the LF growth. At LFs above ∼150, the apoferritin shell undergoes structural changes, which is strongly indicative of the fact that the shell stability is affected by iron oxide presence