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.

中文翻译：

---

淀粉样蛋白 β-肽与铁储存蛋白铁蛋白相互作用后形成 Fe(II)

在体外研究了淀粉样蛋白 β-肽 (Aβ) 与铁储存蛋白铁蛋白的相互作用。我们已经表明，在原纤维形成过程中，Aβ 能够将 Fe(III) 从铁蛋白核（水铁矿）还原为 Fe(II)。Aβ 介导的 Fe(III) 还原产生的游离 Fe(II) 浓度是铁蛋白本身自发形成的 Fe(II) 的两倍。我们建议 Aβ 也可以充当铁蛋白特异性金属伴侣蛋白样分子，从铁蛋白水合铁核中捕获 Fe(III)。我们的观察可能部分解释了患有神经退行性疾病的人类大脑中含 Fe(II) 矿物质的形成。