Silver nanoparticle synthesis in human ferritin by photochemical reduction

Moglia, Italo; Santiago, Margarita; Soler, Mónica; Olivera-Nappa, Álvaro

doi:10.1016/j.jinorgbio.2020.111016

Cited by 17 publications

(6 citation statements)

References 42 publications

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“…ApoFTL exhibits a broad first protein elution with two overlapping peaks at 8.9 and 9.4 mL and a second elution peak at 10.8 mL (Figure 3A). These elution profiles indicate two different subpopulations of ferritin in the original sample that have also been reported by other authors [22,[45][46][47]. The first protein elution peak with a higher molecular weight corresponds to ferritin cage oligomers (dimers or trimers), while the second elution peak contains ferritin cage monomers, corroborated by native PAGE analysis (Figure S1).…”

Section: Gold Nanoparticles Synthesis and Characterizationsupporting

confidence: 86%

“…Both subunit types (H or L) have similar amino acid substitutions that confer functions specific to each subunit [19,20]. Ferritin is completely biocompatible because it is endogenous to humans; its protein shell provides a highly stable protective layer for inorganic nanoparticle coating [17,[21][22][23][24][25][26], and its cavity has been successfully used as a nanoreactor to prepare monodisperse metallic nanoparticles [18,22,27]. The synthesis of AuNP in ferritins from different origins has been reported using horse spleen FT [14][15][16], mutant L-chain horse spleen FT [28], H-chain human FT [17,29], mutant H-chain human FT [30], and Archaeoglobus fulgidus FT [26].…”

Section: Introductionmentioning

confidence: 99%

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Enhanced Cellular Uptake of H-Chain Human Ferritin Containing Gold Nanoparticles

et al. 2021

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Gold nanoparticles (AuNP) capped with biocompatible layers have functional optical, chemical, and biological properties as theranostic agents in biomedicine. The ferritin protein containing in situ synthesized AuNPs has been successfully used as an effective and completely biocompatible nanocarrier for AuNPs in human cell lines and animal experiments in vivo. Ferritin can be uptaken by different cell types through receptor-mediated endocytosis. Despite these advantages, few efforts have been made to evaluate the toxicity and cellular internalization of AuNP-containing ferritin nanocages. In this work, we study the potential of human heavy-chain (H) and light-chain (L) ferritin homopolymers as nanoreactors to synthesize AuNPs and their cytotoxicity and cellular uptake in different cell lines. The results show very low toxicity of ferritin-encapsulated AuNPs on different human cell lines and demonstrate that efficient cellular ferritin uptake depends on the specific H or L protein chains forming the ferritin protein cage and the presence or absence of metallic cargo. Cargo-devoid apoferritin is poorly internalized in all cell lines, and the highest ferritin uptake was achieved with AuNP-loaded H-ferritin homopolymers in transferrin-receptor-rich cell lines, showing more than seven times more uptake than apoferritin.

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Section: Gold Nanoparticles Synthesis and Characterizationsupporting

confidence: 86%

Section: Introductionmentioning

confidence: 99%

Enhanced Cellular Uptake of H-Chain Human Ferritin Containing Gold Nanoparticles

et al. 2021

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“…Moreover, the intrinsic process allows for the production of size-limited metal nanoparticles within the protein's core through a reduction facilitated by NaBH 4 . 92 Furthermore, this structure permits Cu 2+ to bind to the 3-fold channel of apoferritin, resulting in a stable thiol bridge structure reinforced by His and Glu. 93 This promising research paves the way for the creation of enhanced copper supplements based on this chemical transformation process.…”

Section: Transporting Coppermentioning

confidence: 99%

Multifaceted Applications of Ferritin Nanocages in Delivering Metal Ions, Bioactive Compounds, and Enzymes: A Comprehensive Review

Hu,

Sha,

et al. 2023

J. Agric. Food Chem.

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Ferritin, a distinctive iron-storage protein, possesses a unique cage-like nanoscale structure that enables it to encapsulate and deliver a wide range of biomolecules. Recent advances prove that ferritin can serve as an efficient 8 nm diameter carrier for various bioinorganic nutrients, such as minerals, bioactive polyphenols, and enzymes. This review offers a comprehensive summary of ferritin’s structural features from different sources and emphasizes its functions in iron supplementation, calcium delivery, single- and coencapsulation of polyphenols, and enzyme package. Additionally, the influence of innovative food processing technologies, including manothermosonication, pulsed electric field, and atmospheric cold plasma, on the structure and function of ferritin are examined. Furthermore, the limitations and prospects of ferritin in food and nutritional applications are discussed. The exploration of ferritin as a multifunctional protein with the capacity to load various biomolecules is crucial to fully harnessing its potential in food applications.

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“…Similarly, Moglia et al and Douglas et al. have been able to produce highly monodispersed nanoparticles by synthesizing Ag NPs and Co(O)OH NPs inside the ferritin protein via the nanoreactor route, respectively. , Thus, ferritin nanocages not only provided a template for the size selective synthesis of nanoparticles but also prevented the aggregation and bulk precipitation of nanoparticles. Recently, Wang et al have successfully utilized ferritin nanocage as a nanoreactor for synthesizing ∼8 nm sized CuS nanoparticles having excellent biocompatibility and strong absorption in NIR regions required for anticancer applications .…”

Section: Biomedical and Biotechnological Applications Of Ferritins: A...mentioning

confidence: 99%

Ferritin: A Promising Nanoreactor and Nanocarrier for Bionanotechnology

Mohanty

Parida

Raut

et al. 2022

ACS Bio Med Chem Au

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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.

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Silver nanoparticle synthesis in human ferritin by photochemical reduction

Cited by 17 publications

References 42 publications

Enhanced Cellular Uptake of H-Chain Human Ferritin Containing Gold Nanoparticles

Enhanced Cellular Uptake of H-Chain Human Ferritin Containing Gold Nanoparticles

Multifaceted Applications of Ferritin Nanocages in Delivering Metal Ions, Bioactive Compounds, and Enzymes: A Comprehensive Review

Ferritin: A Promising Nanoreactor and Nanocarrier for Bionanotechnology

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