4.6 Article

The Impact of Redox, Hydrolysis and Dehydration Chemistry on the Structural and Magnetic Properties of Magnetoferritin Prepared in Variable Thermal Conditions

Journal

MOLECULES
Volume 26, Issue 22, Pages -

Publisher

MDPI
DOI: 10.3390/molecules26226960

Keywords

magnetoferritin; magnetite; loading factor; protein stability; aqueous medium

Funding

  1. Scientific Grant Agency of the Ministry of Education, Science, Research and Sport of the Slovak Republic
  2. Slovak Academy of Sciences (VEGA) [2/0044/20, 2/0013/19]
  3. Slovak Research and Development Agency [APVV-015-0453, APVV-20-0068, APVV-20-0205, APVV-19-0324]
  4. MVTS MAGBBRIS
  5. MVTS SKTW AMAZON
  6. FMF at Institut Max von Laue-Paul Langevin [PP-COVID-20-0025, 73139]

Ask authors/readers for more resources

Ferritin, a protein complex responsible for iron storage in organisms, has different iron core compositions related to specific living requirements and health states. Magnetoferritin, a synthetic derivative, serves as a model system with unusual iron phase structures. Improving synthesis technology can enhance physicochemical parameters of the system for applications.
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.

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