The essence of bionanotechnology
lies in the application of nanotechnology/nanomaterials
to solve the biological problems. Quantum dots and nanoparticles hold
potential biomedical applications, but their inherent problems such
as low solubility and associated toxicity due to their interactions
at nonspecific target sites is a major concern. The self-assembled,
thermostable, ferritin protein nanocages possessing natural iron scavenging
ability have emerged as a potential solution to all the above-mentioned
problems by acting as nanoreactor and nanocarrier. Ferritins, the
cellular iron repositories, are hollow, spherical, symmetric multimeric
protein nanocages, which sequester the excess of free Fe(II) and synthesize
iron biominerals (Fe2O3·H2O)
inside their ∼5–8 nm central cavity. The electrostatics
and dynamics of the pore residues not only drives the natural substrate
Fe2+ inside ferritin nanocages but also uptakes a set of
other metals ions/counterions during in vitro synthesis
of nanomaterial. The current review aims to report the recent developments/understanding
on ferritin structure (self-assembly, surface/pores electrostatics,
metal ion binding sites) and chemistry occurring inside these supramolecular
protein cages (protein mediated metal ion uptake and mineralization/nanoparticle
formation) along with its surface modification to exploit them for
various nanobiotechnological applications. Furthermore, a better understanding
of ferritin self-assembly would be highly useful for optimizing the
incorporation of nanomaterials via the disassembly/reassembly
approach. Several studies have reported the successful engineering
of these ferritin protein nanocages in order to utilize them as potential
nanoreactor for synthesizing/incorporating nanoparticles and as nanocarrier
for delivering imaging agents/drugs at cell specific target sites.
Therefore, the combination of nanoscience (nanomaterials) and bioscience
(ferritin protein) projects several benefits for various applications
ranging from electronics to medicine.