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.
CITATION STYLE
Balejcikova, L., Siposova, K., Kopcansky, P., & Safarik, I. (2018). Fe(II) formation after interaction of the amyloid β-peptide with iron-storage protein ferritin. Journal of Biological Physics, 44(3), 237–243. https://doi.org/10.1007/s10867-018-9498-3
Mendeley helps you to discover research relevant for your work.