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Updated: Feb 10, 2026

Identifying Protein-protein Interaction Sites Using Peptide Arrays
Published on: November 18, 2014
Fe(II) formation after interaction of the amyloid β-peptide with iron-storage protein ferritin
Lucia Balejcikova1, Katarina Siposova1, Peter Kopcansky1
1Institute of Experimental Physics, SAS, Watsonova 47, 040 01, Kosice, Slovakia.
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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