Use of nucleic acids anchor system to reveal apoferritin modification by cadmium telluride nanoparticles

Kudr, Jiří; Nejdl, Lukáš; Skaličková, Sylvie; Žůrek, Michal; Milosavljević, Vedran; Kenšová, Renáta; Ruttkay-Nedecký, Branislav; Kopel, Pavel; Hynek, David; Novotná, Marie; Adam, Vojtěch; Kizek, René

doi:10.1039/c4tb01336k

Cited by 9 publications

(6 citation statements)

References 74 publications

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“…Polycharged magnetic particles modified by a surface-coating either with silica, polyvinylpyrrolidone or tripolyphosphate are easy to make in the laboratory and have demonstrated interactions with DNA for magnetic isolation applications [ 38 ]. Sequence specific isolation of nucleic acids can be performed using magnetic particles decorated with oligonucleotide probes which recognize target nucleic acid according to its sequence [ 175 , 176 ]. Adams et al, compared abilities of commercially available magnetic particles for isolation of RNA—silica coated, particles decorated with a polythymine oligonucleotide probe (oligo (dT)) and particles functionalized with an oligonucleotide complementary to target sequence [ 177 ].…”

Section: Magnetic Nanoparticles In the Real Worldmentioning

confidence: 99%

Magnetic Nanoparticles: From Design and Synthesis to Real World Applications

et al. 2017

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The increasing number of scientific publications focusing on magnetic materials indicates growing interest in the broader scientific community. Substantial progress was made in the synthesis of magnetic materials of desired size, morphology, chemical composition, and surface chemistry. Physical and chemical stability of magnetic materials is acquired by the coating. Moreover, surface layers of polymers, silica, biomolecules, etc. can be designed to obtain affinity to target molecules. The combination of the ability to respond to the external magnetic field and the rich possibilities of coatings makes magnetic materials universal tool for magnetic separations of small molecules, biomolecules and cells. In the biomedical field, magnetic particles and magnetic composites are utilized as the drug carriers, as contrast agents for magnetic resonance imaging (MRI), and in magnetic hyperthermia. However, the multifunctional magnetic particles enabling the diagnosis and therapy at the same time are emerging. The presented review article summarizes the findings regarding the design and synthesis of magnetic materials focused on biomedical applications. We highlight the utilization of magnetic materials in separation/preconcentration of various molecules and cells, and their use in diagnosis and therapy.

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Section: Magnetic Nanoparticles In the Real Worldmentioning

confidence: 99%

Magnetic Nanoparticles: From Design and Synthesis to Real World Applications

et al. 2017

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“…Indeed, ferritin and apoferritin have proved to be very heat resistant. Using UV-Vis spectrophotometry and gel electrophoresis 25 to investigate the thermostability of horse spleen apoferritin, Kudr et al (2015) report small conformational changes already at 36°C. Above 65°C, the spherical cage structure is lost, accompanied by the release of subunits.…”

Section: Stress Treatmentsmentioning

confidence: 99%

Protein aggregates nucleate ice: the example of apoferritin

Cascajo-Castresana¹,

David²,

Iriarte-Alonso³

et al. 2019

Preprint

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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 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 >&#8201;0.1&#8201;mg&#8722;1 at 10&#8201;&#176;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&#8201;mg&#8722;1 at 14&#8201;&#176;C to 10,000&#8201;mg&#8722;1 at &#8722;20&#8201;&#176;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 >&#8201;10&#8201;mg&#8722;1 at &#8722;5&#8201;&#176;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 &#8722;4 to &#8722;11&#8201;&#176;C and a lower one from &#8722;11 to &#8722;21&#8201;&#176;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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“…A lattice match between ice and the ice-nucleating agent is often considered a prerequisite for heterogeneous ice nucleation. Yet, while some IN-active substances such as AgI (Marcolli et al, 2016) and 2D-crystalline films formed by long-chain alcohols (Popovitz-Biro et al, 1994;Zobrist et al, 2007;Qiu et al, 2017) exhibit a lattice match, others such as quartz (Kumar et al, 2019a) do not, and even others such as BaF 2 exhibit a lattice match but fail to be IN active (Conrad et al, 2005). The difficulty to pinpoint surface properties that are required for heterogeneous ice nucleation may be explained by growing evidence that it is not the whole surface that is able to nucleate ice but just special nucleation sites (Vali, 2014;Vali et al, 2015), which may arise through defects or impurities.…”

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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Use of nucleic acids anchor system to reveal apoferritin modification by cadmium telluride nanoparticles

Abstract: The aim of this study was to synthesize cadmium telluride nanoparticles (CdTe NPs) modified apoferritin, and examine if apoferritin is able to accommodate CdTe NPs.

Cited by 9 publications

References 74 publications

Magnetic Nanoparticles: From Design and Synthesis to Real World Applications

Magnetic Nanoparticles: From Design and Synthesis to Real World Applications

Protein aggregates nucleate ice: the example of apoferritin

Protein aggregates nucleate ice: the example of apoferritin

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