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Ferritin Nanocage: A Versatile Nanocarrier Utilized in the Field of Food, Nutrition, and Medicine.

ABSTRACT: Compared with other nanocarriers such as liposomes, mesoporous silica, and cyclodextrin, ferritin as a typical protein nanocage has received considerable attention in the field of food, nutrition, and medicine owing to its inherent cavity size, excellent water solubility, and biocompatibility. Additionally, ferritin nanocage also serves as a versatile bio-template for the synthesis of a variety of nanoparticles. Recently, scientists have explored the ferritin nanocage structure for encapsulation and delivery of guest molecules such as nutrients, bioactive molecules, anticancer drugs, and mineral metal ions by taking advantage of its unique reversible disassembly and reassembly property and biomineralization. In this review, we mainly focus on the preparation and structure of ferritin-based nanocarriers, and regulation of their self-assembly. Moreover, the recent advances of their applications in food nutrient delivery and medical diagnostics are highlighted. Finally, the main challenges and future development in ferritin-directed nanoparticles' synthesis and multifunctional applications are discussed.

SUBMITTER: Zhang C

PROVIDER: S-EPMC7557750 | biostudies-literature | 2020 Sep

REPOSITORIES: biostudies-literature

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Ferritin Nanocage: A Versatile Nanocarrier Utilized in the Field of Food, Nutrition, and Medicine.

Zhang Chenxi C Zhang Xiaorong X Zhao Guanghua G

Nanomaterials (Basel, Switzerland) 20200922 9

Compared with other nanocarriers such as liposomes, mesoporous silica, and cyclodextrin, ferritin as a typical protein nanocage has received considerable attention in the field of food, nutrition, and medicine owing to its inherent cavity size, excellent water solubility, and biocompatibility. Additionally, ferritin nanocage also serves as a versatile bio-template for the synthesis of a variety of nanoparticles. Recently, scientists have explored the ferritin nanocage structure for encapsulation ...[more]

PMID: 32971961

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Project description: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.

Project description:The bottom-up self-assembly of protein subunits into supramolecular nanoarchitectures is ubiquitously exploited to recapitulate and expand the features of natural proteins to advance nanoscience in medicine. Various chemical and biological re-engineering approaches are available to render diverse functions in the given proteins. They are, unfortunately, capable of compromising protein integrity and stability after extensive modifications. In this study, we introduce a new protein re-engineering method, metal ion assisted interface re-engineering (MAIR), to serve as a robust and universal strategy to extend the functions of self-assembly proteins by boosting structural features to advance their diverse biomedical applications. In particular, the MAIR strategy was applied to a widely used natural protein, ferritin, as a model protein to coordinate with copper ions in its mutagenic artificial metal binding domain. Structure directed rational protein mutagenesis was carried out at the C2 interface amino acid residues of the ferritin subunit for metal ion coordination site optimization. Copper binding at the artificial binding pocket was highly specific over the other divalent ions present in physiological fluids, and the structurally embedded copper ion in turn strengthened the overall protein integrity and stability. In the presence of isotopic copper-64, the interface re-engineered ferritin worked as a chelator-free molecular nanoprobe with an extraordinarily high specific activity to allow PET imaging of tumors in live animals. We also found that the re-engineered ferritin coordinating with copper ions demonstrates high drug loading capacity of a widely used anti-cancer agent, doxorubicin (DOX), to achieve significant drug retention at the tumor site and enhance tumor regression for improved anti-cancer effects. The MAIR approach, thus, exploited the copper ion to facilitate efficient one-step labeling of mutant ferritin derivatives for simultaneous molecular imaging and drug delivery. The reported interface re-engineering strategy provides an unparalleled opportunity to expand protein biofunctions to serve as a new theranostic agent in cancer research.

Dataset Information

Ferritin Nanocage: A Versatile Nanocarrier Utilized in the Field of Food, Nutrition, and Medicine.

Publications

Ferritin Nanocage: A Versatile Nanocarrier Utilized in the Field of Food, Nutrition, and Medicine.

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