Bence-Jones protein as the form of nano-scaled β-stacked supramolecular aggregates

Voroshylova, Natalia; Timchenko, Мarina D.; Verevka, Serhij

doi:10.31450/ukrjnd.1(61).2019.05

Cited by 3 publications

(1 citation statement)

References 19 publications

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“…This, however, did not exclude the possibility of their formation in micro-and nanoscale dimensiom, that are invisible in solution. In the presence of β-folded structures in their composition, they may be detected by precipitation by Congo Red (Buxbaum & Linke, 2012;Voroshylova et al, 2019). Due to incubation with Congo red for two days at room temperature, the formation of dark red precipitates was observed.…”

Section: Introductionmentioning

confidence: 99%

Metal-Induced Protein Denaturation: Regularities, Pathological Manifestations, and in Vitro Modeling

Popovych

Kizim

Obernikhina

et al. 2021

USMYJ

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the ability of various metal ions to form complexes with proteins leads to the denaturation of the latter and the development of immune response. Such hapten effects cause the well-known phenomenon of nickel-allergic contact dermatitis. No less typical are side effects of gadolinium compounds, that are used as contrasts for magnetic resonance imaging, but cause the development of fibrosis. In both cases an important role belongs to the interaction of metal ions with collagen structures. The aim of our study was to compare in vitro effects of copper and nickel ions on destabilized products of collagen cleavage. Significant difference between these metals in their ability to induce aggregation at close to physiological pH values was shown. The influence on the aggregative process of the acidification of the medium was revealed. It was shown that destabilization of protein structure leads to the formation of highly stabilized β-stacked protein aggregates. Comparison of the obtained experimental data with the literature ones makes it possible to approach the understanding of individual mechanisms of toxic effects of metal ions on the human body.

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Section: Introductionmentioning

confidence: 99%

Metal-Induced Protein Denaturation: Regularities, Pathological Manifestations, and in Vitro Modeling

Popovych

Kizim

Obernikhina

et al. 2021

USMYJ

View full text Add to dashboard Cite

show abstract

Metal-Induced Protein Denaturation: Regularities, Pathological Manifestations, and in Vitro Modeling

Popovych,

Kizim,

Obernikhina

et al. 2021

USMYJ

View full text Add to dashboard Cite

the ability of various metal ions to form complexes with proteins leads to the denaturation of the latterand the development of immune response. Such hapten effects cause the well-known phenomenon of nickel-allergiccontact dermatitis. No less typical are side effects of gadolinium compounds, that are used as contrasts for magneticresonance imaging, but cause the development of fibrosis. In both cases an important role belongs to the interactionof metal ions with collagen structures. The aim of our study was to compare in vitro effects of copper and nickel ionson destabilized products of collagen cleavage. Significant difference between these metals in their ability to induce aggregation at close to physiological pH values was shown. The influence on the aggregative process of the acidifica-tion of the medium was revealed. It was shown that destabilization of protein structure leads to the formation of highly stabilized β-stacked protein aggregates. Comparison of the obtained experimental data with the literature ones makesit possible to approach the understanding of individual mechanisms of toxic effects of metal ions on the human body.

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Fibrosis: Polyetiologic Complication With Common Denominator

Zabolotnyi¹,

Dieieva²,

Gurzhenko³

et al. 2021

Journal NAMSU

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State of the problem. The growth of fibrous connective tissue is a common complication of various pathological processes, which significantly complicates recovery and is one of the leading causes of death. Despite many years of research, the process of fibrosis development remains insufficiently studied and contains a large number of “white spots”. Fibrosis is characterized by unpredictability, propensity to grow and low level of the replacement by normal connective tissue. The structure of fibrous tissue, its differences from normal and the reasons for the formation of these differences deserve no less attention. The formation of fibrous tissue is preceded by the process of endogenous intoxication – the formation and accumulation of various abnormal metabolites. Among the latter, the leading place belongs to proteins and peptides, whose structure is disrupted and destabilized. It is known that destabilized proteins are prone to aggregation. This process, contrary to popular belief, is not chaotic, but is subject to certain laws and is aimed at minimizing of free energy. With regard of the latter circumstance a definite favorite is the formation of β-structured fibrils, which occupy almost the lowest energy level among protein conformational states. Such fibrils are characterized by insolubility, resistance to proteolysis, immunogenicity and the ability to autochthonous growth due to sorption and conformational rearrangement of soluble proteins. A classic example of such aggregation is amyloid formation, but there are good reasons to assume similar processes in the formation of other pathological tissues. The aim of the work was to verify experimentally the presence of β-structured protein aggregates in fibrous tissues, which differ in etiology. The methodical part included the selection of surgical material, its fixation in 10 % formaldehyde solution, preparation of Congo-stained red histological specimens and microscopic examination in light, polarization and fluorescence modes. Results. The presence of β-structured protein aggregates in fibrous tissues formed due to local chronic inflammation, viral infection and side effects of drugs has been proven experimentally. The identified phenomenon allows us to approach the understanding of the mechanisms of fibrosis development and to postulate a key role of regular aggregation of destabilized proteins. Conclusions. The obtained data testifies to a general and integral participation of β-structured protein aggregates in the formation of fibrous tissues of different etiologies. The presence of these deposits in fibrous tissues formed due to local chronic inflammation, viral infection and side effects of the cytostatic doxorubicin has been shown. The leading role of violation of protein homeostasis and local accumulation of structurally damaged proteins as a prerequisite for autochthonous aggregation process is discussed. The expediency of fluorescence microscopy has been shown, which significantly expands the possibilities of detecting with the help of the Congo red of nanosized β-structured protein aggregates, which are invisible due to Abbe's limitations in light and polarization microscopy. Key words: fibrosis, keloidosis, Peyronie’s disease, Covid-19, cytostatics, nanoparticles.

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Bence-Jones protein as the form of nano-scaled β-stacked supramolecular aggregates

Cited by 3 publications

References 19 publications

Metal-Induced Protein Denaturation: Regularities, Pathological Manifestations, and in Vitro Modeling

Metal-Induced Protein Denaturation: Regularities, Pathological Manifestations, and in Vitro Modeling

Metal-Induced Protein Denaturation: Regularities, Pathological Manifestations, and in Vitro Modeling

Fibrosis: Polyetiologic Complication With Common Denominator

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