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

The interaction of amyloid beta-peptide (A beta) with the iron-storage protein ferritin was studied in vitro. We have shown that A beta during fibril formation process is able to reduce Fe(III) from the ferritin core (ferrihydrite) to Fe(II). The A beta-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 A beta 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.