Enrichment and characterization of ferritin for nanomaterial applications

Ghirlando, Rodolfo; Mutskova, Radina; Schwartz, Chad

doi:10.1088/0957-4484/27/4/045102

Cited by 13 publications

(17 citation statements)

References 44 publications

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“…The relaxivity of ferritin nanoparticles is strongly dependent on the amount of Fe contained in the apoferritin shell [21,94,95]. The iron nanoparticles, stored in the ferritin cages, are either in an antiferromagnetic or super paramagnetic form [96,97], which results in an unique effect on the relaxation of water as detected by MRI [98].…”

Section: Ferritin Nanoparticles Used In Molecular Imagingmentioning

confidence: 99%

“…The ferritin nanoparticles used in constrained synthesis, nanodevices [5,17–21], have been summarized in several excellent review articles and will not be discussed here. In this article, we will focus on the use of ferritin nanoparticles in the fields of drug delivery, vaccine development, bioassay, disease diagnosis and therapy with molecular imaging methods (Fig.…”

Section: Introductionmentioning

confidence: 99%

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Functional ferritin nanoparticles for biomedical applications

Wang

Gao

Zhang

et al. 2017

Front. Chem. Sci. Eng.

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Ferritin, a major iron storage protein with a hollow interior cavity, has been reported recently to play many important roles in biomedical and bioengineering applications. Owing to the unique architecture and surface properties, ferritin nanoparticles offer favorable characteristics and can be either genetically or chemically modified to impart functionalities to their surfaces, and therapeutics or probes can be encapsulated in their interiors by controlled and reversible assembly/disassembly. There has been an outburst of interest regarding the employment of functional ferritin nanoparticles in nanomedicine. This review will highlight the recent advances in ferritin nanoparticles for drug delivery, bioassay, and molecular imaging with a particular focus on their biomedical applications.

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Section: Ferritin Nanoparticles Used In Molecular Imagingmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Functional ferritin nanoparticles for biomedical applications

Wang

Gao

Zhang

et al. 2017

Front. Chem. Sci. Eng.

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“…Heterogeneous ice nucleation is considered to arise from the ability of surfaces to order water molecules in an icelike pattern. The arrangement of water molecules at a surface depends on surface charge and functional groups (Glatz and Sarupria, 2016;Abdelmonem et al, 2017;. A relevant role is attributed to surface OH and NH groups that are able to form hydrogen bonds to water molecules.…”

Section: Introductionmentioning

confidence: 99%

Protein aggregates nucleate ice: the example of apoferritin

et al. 2020

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Abstract. Biological material has gained increasing attention recently as a source of ice-nucleating particles that may account for cloud glaciation at moderate supercooling. While the ice-nucleation (IN) ability of some bacteria can be related to membrane-bound proteins with epitaxial fit to ice, little is known about the IN-active entities present in biological material in general. To elucidate the potential of proteins and viruses to contribute to the IN activity of biological material, we performed bulk freezing experiments with the newly developed drop freezing assay DRoplet Ice Nuclei Counter Zurich (DRINCZ), which allows the simultaneous cooling of 96 sample aliquots in a chilled ethanol bath. We performed a screening of common proteins, namely the iron storage protein ferritin and its iron-free counterpart apoferritin, the milk protein casein, the egg protein ovalbumin, two hydrophobins, and a yeast ice-binding protein, all of which revealed IN activity with active site densities > 0.1 mg−1 at −10 ∘C. The tobacco mosaic virus, a plant virus based on helically assembled proteins, also proved to be IN active with active site densities increasing from 100 mg−1 at −14 ∘C to 10 000 mg−1 at −20 ∘C. Among the screened proteins, the IN activity of horse spleen ferritin and apoferritin, which form cages of 24 co-assembled protein subunits, proved to be outstanding with active site densities > 10 mg−1 at −5 ∘C. Investigation of the pH dependence and heat resistance of the apoferritin sample confirmed the proteinaceous nature of its IN-active entities but excluded the correctly folded cage monomer as the IN-active species. A dilution series of apoferritin in water revealed two distinct freezing ranges, an upper one from −4 to −11 ∘C and a lower one from −11 to −21 ∘C. Dynamic light scattering measurements related the upper freezing range to ice-nucleating sites residing on aggregates and the lower freezing range to sites located on misfolded cage monomers or oligomers. The sites proved to persist during several freeze–thaw cycles performed with the same sample aliquots. Based on these results, IN activity seems to be a common feature of diverse proteins, irrespective of their function, but arising only rarely, most probably through defective folding or aggregation to structures that are IN active.

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confidence: 87%

“…Ferritin proteinscan self-assemble into multi-subunit, nano-scale cages. They are also highly amenable through genetic and chemical modifications, which have attracted much recent attention in drug delivery studies and nanomaterial science [6]. In our previous research, site-directed mutagenesis on N-and C-termini of ferritin 3kx9 led to an increase in the volume of self-assembled protein cages [7].…”

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confidence: 99%

Numerical Study on the Relationship between the Number of Ferritin Subunits and the Size of Outer Diameter

Zhao¹,

Gao²

2018

ABB

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Ferritin is assembled from sub-chains into a spherical shape. We have found that the number of sub-chains is generally 3,6,8, 12, 24, 36, and the corresponding spherical volume (outer diameter) is also different. In this paper, using the protein structural data from PDB website, linear regression was carried out to model the relationship between sub-chain number and outer diameter of 25 ferritins by calculation and analysis, but the results were not ideal. In order to improve the model, we divided the 25 proteins into two groups by molecular evolution, followed by the establishment of a linear model. The correlation coefficient of one group was R 2 = 0.98. Based on calculations and modelling, we hypothesize that the new ferritin formed by the 3kx9 site-directed mutagenesis is no longer 24-chain, but a 36-chain mutant.

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Enrichment and characterization of ferritin for nanomaterial applications

Cited by 13 publications

References 44 publications

Functional ferritin nanoparticles for biomedical applications

Functional ferritin nanoparticles for biomedical applications

Protein aggregates nucleate ice: the example of apoferritin

Numerical Study on the Relationship between the Number of Ferritin Subunits and the Size of Outer Diameter

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