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The Impact of Redox, Hydrolysis and Dehydration Chemistry on the Structural and Magnetic Properties of Magnetoferritin Prepared in Variable Thermal Conditions
Ferritin, a spherically shaped protein complex, is responsible for iron storage in bacteria, plants, animals, and humans. Various ferritin iron core compositions in organisms are associated with specific living requirements, health state, and different biochemical roles of ferritin isomers. Magnetof...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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MDPI
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8619319/ https://www.ncbi.nlm.nih.gov/pubmed/34834056 http://dx.doi.org/10.3390/molecules26226960 |
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author | Balejčíková, Lucia Saksl, Karel Kováč, Jozef Martel, Anne Garamus, Vasil M. Avdeev, Mikhail V. Petrenko, Viktor I. Almásy, László Kopčanský, Peter |
author_facet | Balejčíková, Lucia Saksl, Karel Kováč, Jozef Martel, Anne Garamus, Vasil M. Avdeev, Mikhail V. Petrenko, Viktor I. Almásy, László Kopčanský, Peter |
author_sort | Balejčíková, Lucia |
collection | PubMed |
description | Ferritin, a spherically shaped protein complex, is responsible for iron storage in bacteria, plants, animals, and humans. Various ferritin iron core compositions in organisms are associated with specific living requirements, health state, and different biochemical roles of ferritin isomers. Magnetoferritin, a synthetic ferritin derivative, serves as an artificial model system of unusual iron phase structures found in humans. We present the results of a complex structural study of magnetoferritins prepared by controlled in vitro synthesis. Using various complementary methods, it was observed that manipulation of the synthesis technology can improve the physicochemical parameters of the system, which is useful in applications. Thus, a higher synthesis temperature leads to an increase in magnetization due to the formation of the magnetite phase. An increase in the iron loading factor has a more pronounced impact on the protein shell structure in comparison with the pH of the aqueous medium. On the other hand, a higher loading factor at physiological temperature enhances the formation of an amorphous phase instead of magnetite crystallization. It was confirmed that the iron-overloading effect alone (observed during pathological events) cannot contribute to the formation of magnetite. |
format | Online Article Text |
id | pubmed-8619319 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-86193192021-11-27 The Impact of Redox, Hydrolysis and Dehydration Chemistry on the Structural and Magnetic Properties of Magnetoferritin Prepared in Variable Thermal Conditions Balejčíková, Lucia Saksl, Karel Kováč, Jozef Martel, Anne Garamus, Vasil M. Avdeev, Mikhail V. Petrenko, Viktor I. Almásy, László Kopčanský, Peter Molecules Article Ferritin, a spherically shaped protein complex, is responsible for iron storage in bacteria, plants, animals, and humans. Various ferritin iron core compositions in organisms are associated with specific living requirements, health state, and different biochemical roles of ferritin isomers. Magnetoferritin, a synthetic ferritin derivative, serves as an artificial model system of unusual iron phase structures found in humans. We present the results of a complex structural study of magnetoferritins prepared by controlled in vitro synthesis. Using various complementary methods, it was observed that manipulation of the synthesis technology can improve the physicochemical parameters of the system, which is useful in applications. Thus, a higher synthesis temperature leads to an increase in magnetization due to the formation of the magnetite phase. An increase in the iron loading factor has a more pronounced impact on the protein shell structure in comparison with the pH of the aqueous medium. On the other hand, a higher loading factor at physiological temperature enhances the formation of an amorphous phase instead of magnetite crystallization. It was confirmed that the iron-overloading effect alone (observed during pathological events) cannot contribute to the formation of magnetite. MDPI 2021-11-18 /pmc/articles/PMC8619319/ /pubmed/34834056 http://dx.doi.org/10.3390/molecules26226960 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Balejčíková, Lucia Saksl, Karel Kováč, Jozef Martel, Anne Garamus, Vasil M. Avdeev, Mikhail V. Petrenko, Viktor I. Almásy, László Kopčanský, Peter The Impact of Redox, Hydrolysis and Dehydration Chemistry on the Structural and Magnetic Properties of Magnetoferritin Prepared in Variable Thermal Conditions |
title | The Impact of Redox, Hydrolysis and Dehydration Chemistry on the Structural and Magnetic Properties of Magnetoferritin Prepared in Variable Thermal Conditions |
title_full | The Impact of Redox, Hydrolysis and Dehydration Chemistry on the Structural and Magnetic Properties of Magnetoferritin Prepared in Variable Thermal Conditions |
title_fullStr | The Impact of Redox, Hydrolysis and Dehydration Chemistry on the Structural and Magnetic Properties of Magnetoferritin Prepared in Variable Thermal Conditions |
title_full_unstemmed | The Impact of Redox, Hydrolysis and Dehydration Chemistry on the Structural and Magnetic Properties of Magnetoferritin Prepared in Variable Thermal Conditions |
title_short | The Impact of Redox, Hydrolysis and Dehydration Chemistry on the Structural and Magnetic Properties of Magnetoferritin Prepared in Variable Thermal Conditions |
title_sort | impact of redox, hydrolysis and dehydration chemistry on the structural and magnetic properties of magnetoferritin prepared in variable thermal conditions |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8619319/ https://www.ncbi.nlm.nih.gov/pubmed/34834056 http://dx.doi.org/10.3390/molecules26226960 |
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