Its hollow spherical structure that naturally stores iron ions has been diversely exploited by researchers in biotherapeutics 4. Moreover, the large surface-to-volume ratio and the disassembly/reassembly feature of the 24 monomer subunits into a sphere allow diverse modifications on the surface and inner cage of ferritin by chemical and genetic methods. Ferritin has excellent biosafety profiles, and the nanosized particles exhibit rapid dispersion and controlled/sustained release pharmacokinetics. In this review, we highlight ferritin nanocages.įerritin exists in almost all living organisms, participating in iron homeostasis by storing and releasing iron ions 3. Due to these advantages, diverse types of protein nanocarriers have been highlighted for their inherent biodegradability and ease of genetic modification compared to other types of nanocarriers 2. They are also cleared from circulation relatively slowly, which allows controlled/sustained drug release in targeted sites. Furthermore, protein nanocarriers have improved the targeted delivery and pharmacokinetic profiles of drug cargo. Their nanometer size range allows advantageous properties that permit diverse modifications, such as surface functionalization, and enable the rapid dispersion of loaded drugs. The exploitation of protein nanocarriers has played a vital role in advancing disease diagnosis and therapy 1. This golden shortlist of recent developments will be of immediate benefit and interest to researchers studying ferritin and other protein-based biotherapeutics. Although there are no currently approved drugs based on ferritin, this multifunctional protein scaffold shows immense potential in drug development in diverse categories, and ferritin-based drugs have recently entered phase I clinical trials. We (i) introduce the application of ferritin in drug delivery (ii) present an overview of the use of ferritin in imaging and diagnosis for biomedical purposes (iii) discuss ferritin-based vaccines and (iv) review ferritin-based agents currently in clinical trials. Here, we critically review ferritin and its applications. Moreover, the large surface-to-volume ratio and the disassembly/reassembly behavior of the 24 monomer subunits into a sphere allow diverse modifications by chemical and genetic methods on the surface and inner cage of ferritin. Its hollow spherical structure that naturally stores iron ions has been diversely exploited by researchers in biotherapeutics. The ferritin nanocage is an endogenous protein that exists in almost all mammals.

Protein scaffold minimal