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.

Department of Nanobiotechnology Biology Centre ISB CAS Na Sadkach 7 370 05 Ceske Budejovice Czech Republic

Institute of Experimental Physics SAS Watsonova 47 040 01 Kosice Slovakia

Regional Centre of Advanced Technologies and Materials Palacky University Slechtitelu 27 783 71 Olomouc Czech Republic

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