The effect of solution pH on the structural stability of magnetoferritin

Balejčíková, Lucia; Garamus, V. M.; Авдеев, М. В.; Петренко, В. И.; Almásy, László; Kopčanský, P.

doi:10.1016/j.colsurfb.2017.05.036

Cited by 13 publications

(13 citation statements)

References 47 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…4b, c). Therefore, the electrostatic repulsion between AU net charges is not significant under the conditions in which μ is > 0.1 and is not a serious problem for the assembly under physiological conditions (intracellular solutions contain 140 mM potassium ions) (Alberts et al 2002). Rather, local electrostatic repulsions between charges located near the AU interface seem to be important.…”

Section: Assembly Reactions Of Net-charge Mutantsmentioning

confidence: 96%

“…The pH-dependent dissociation and reassembly were also studied by SAXS (Kim et al 2011). SAXS is also useful to study the morphology of iron mineral core, its formation, and iron release process (Balejcikova et al 2017;Ciasca et al 2012;Fischbach and Anderegg 1965;Gálvez et al 2008;Kim et al 2011;Melnikova et al 2014). All of these studies were performed using HSF and encountered some experimental difficulties such as irreversibility of dissociation, aggregate formation, or destruction of the sell structure upon iron loading.…”

Section: Other Saxs Studies On Ferritinsmentioning

confidence: 99%

See 1 more Smart Citation

Mechanisms of ferritin assembly studied by time-resolved small-angle X-ray scattering

Sato

Ikeguchi

2019

Biophys Rev

View full text Add to dashboard Cite

The assembly reaction of Escherichia coli ferritin A (EcFtnA) was studied using time-resolved small-angle X-ray scattering (SAXS). EcFtnA forms a cage-like structure that consists of 24 identical subunits and dissociates into dimers at acidic pH. The dimer maintains native-like secondary and tertiary structures and can reassemble into a 24-mer when the pH is increased. The time-dependent changes in the SAXS profiles of ferritin during its assembly were roughly explained by a simple model in which only tetramers, hexamers, and dodecamers were considered intermediates. The rate of assembly increased with increasing ionic strength and decreased with increasing pH (from pH 6 to pH 8). These tendencies might originate from repulsion between assembly units (dimers) with the same net charge sign. To test this hypothesis, ferritin mutants with different net charges (netcharge mutants) were prepared. In buffers with low ionic strength, the rate of assembly increased with decreasing net charge. Thus, repulsion between the assembly unit net charges was an important factor influencing the assembly rate. Although the differences in the assembly rate among net-charge mutants were not significant in buffers with an ionic strength higher than 0.1, the assembly rates increased with increasing ionic strength, suggesting that local electrostatic interactions are also responsible for the ionic-strength dependence of the assembly rate and are, on average, repulsive.

show abstract

Section: Assembly Reactions Of Net-charge Mutantsmentioning

confidence: 96%

Section: Other Saxs Studies On Ferritinsmentioning

confidence: 99%

Mechanisms of ferritin assembly studied by time-resolved small-angle X-ray scattering

Sato

Ikeguchi

2019

Biophys Rev

View full text Add to dashboard Cite

show abstract

“…S14†). In consideration of the isoelectric point of apoferritin, more acidic pH was not applied to avoid protein precipitation 48. As shown in Fig.…”

mentioning

confidence: 99%

Iron sulfur clusters in protein nanocages for photocatalytic hydrogen generation in acidic aqueous solutions

Chen

Xiao

et al. 2019

Chem. Sci.

View full text Add to dashboard Cite

show abstract

“…To achieve magnetite crystallization in the middle of the synthesis of MF, 2 M NaOH solution was added [28] to prevent the lepidocrocite crystallization that was observed in samples prepared by the standard MF synthetic procedure [29]. The change in pH increased the magnetization, but it also probably partially destroyed the protein coat, as proved in a recent study [27]. Uncoated mineral cores can thus interact with each other forming larger aggregates which were observed, for example, in neurodegenerative diseases [9,10].…”

Section: Resultsmentioning

confidence: 99%

“…However, the higher ζ potential and PDI in MF does not mean the samples are unstable. The presence of some monodisperse particles is not excluded; this was demonstrated by the pH variation (changing to lower values indicates the presence of core-shell structures) and by Small-Angle X-ray Scattering (SAXS) [27]. MF samples were prepared to mimic magnetite mineralization and aggregation, which have been found in various pathological processes.…”

Section: Resultsmentioning

confidence: 99%

Longitudinal and Transverse Relaxivity Analysis of Native Ferritin and Magnetoferritin at 7 T MRI

Štrbák

Balejčíková

Kmetova

et al. 2021

IJMS

View full text Add to dashboard Cite

Magnetite mineralization in human tissue is associated with various pathological processes, especially neurodegenerative disorders. Ferritin’s mineral core is believed to be a precursor of magnetite mineralization. Magnetoferritin (MF) was prepared with different iron loading factors (LFs) as a model system for pathological ferritin to analyze its MRI relaxivity properties compared to those of native ferritin (NF). The results revealed that MF differs statistically significantly from NF, with the same LF, for all studied relaxation parameters at 7 T: r1, r2, r2*, r2/r1, r2*/r1. Distinguishability of MF from NF may be useful in non-invasive MRI diagnosis of pathological processes associated with iron accumulation and magnetite mineralization (e.g., neurodegenerative disorders, cancer, and diseases of the heart, lung and liver). In addition, it was found that MF samples possess very strong correlation and MF’s relaxivity is linearly dependent on the LF, and the transverse and longitudinal ratios r2/r1 and r2*/r1 possess complementary information. This is useful in eliminating false-positive hypointensive artefacts and diagnosis of the different stages of pathology. These findings could contribute to the exploitation of MRI techniques in the non-invasive diagnosis of iron-related pathological processes in human tissue.

show abstract

The effect of solution pH on the structural stability of magnetoferritin

Cited by 13 publications

References 47 publications

Mechanisms of ferritin assembly studied by time-resolved small-angle X-ray scattering

Mechanisms of ferritin assembly studied by time-resolved small-angle X-ray scattering

Iron sulfur clusters in protein nanocages for photocatalytic hydrogen generation in acidic aqueous solutions

Longitudinal and Transverse Relaxivity Analysis of Native Ferritin and Magnetoferritin at 7 T MRI

Contact Info

Product

Resources

About