Fe(II) formation after interaction of the amyloid β-peptide with iron-storage protein ferritin

Abstract

The interaction of amyloid β-peptide (Aβ) with the iron-storage protein ferritin was studied in vitro. We have shown that Aβ during fibril formation process is able to reduce Fe(III) from the ferritin core (ferrihydrite) to Fe(II). The Aβ-mediated Fe(III) reduction yielded a two-times-higher concentration of free Fe(II) than the spontaneous formation of Fe(II) by the ferritin itself. We suggest that Aβ can also act as a ferritin-specific metallochaperone-like molecule capturing Fe(III) from the ferritin ferrihydrite core. Our observation may partially explain the formation of Fe(II)-containing minerals in human brains suffering by neurodegenerative diseases.

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Acknowledgements

This work was supported by VEGA Grant Agency (project No. 2/0062/16, 2/0016/17, 0045, 2/0062/14, 2/0009/17), the Slovak Research and Development Agency (contract No. APVV-015-0453) and the Ministry of Education Agency for European Structural Funds (projects No. 26220120021, 2622012033, 26220220061, and 26220220186).

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Correspondence to Ivo Safarik.

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Balejcikova, L., Siposova, K., Kopcansky, P. et al. Fe(II) formation after interaction of the amyloid β-peptide with iron-storage protein ferritin. J Biol Phys 44, 237–243 (2018). https://doi.org/10.1007/s10867-018-9498-3

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Keywords

  • Ferritin
  • Aβ
  • Iron reduction
  • Alzheimer’s disease
  • Magnetite
  • Metallochaperone