Ferritin, a natural iron storage protein, is endowed with a unique structure, the ability to self-assemble and excellent physicochemical properties. Beyond these, genetic manipulation can easily tune the structure and functions of ferritin nanocages, which further expands the biomedical applications of ferritin. Here, we focus on human H-ferritin, a recently discovered ligand of transferrin receptor 1, to review its derived variants and related structures and properties. We hope this review will provide new insights into how to rationally design versatile protein cage nanocarriers for effective disease treatment.
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Jin et al. (2019) studied this question.
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