The accumulation of iron oxides - mainly magnetite - with amyloid peptide is a key process in the development of Alzheimer's disease (AD). However, the mechanism for biogeneration of magnetite inside the brain of someone with AD is still unclear. The iron-storing protein ferritin has been identified as the main magnetite-storing molecule. However, accumulations of magnetite in AD are not correlated with an increase in ferritin, leaving this question unresolved. Here we demonstrate the key role of amyloid peptide AÎ² 42, one of the main hallmarks of AD, in the generation of magnetite nanoparticles in the absence of ferritin. The capacity of amyloid peptide to bind and concentrate iron hydroxides, the basis for the formation of magnetite, benefits the spontaneous synthesis of these nanoparticles, even under unfavorable conditions for their formation. Using scanning and transmission electron microscopy, electron energy loss spectroscopy and magnetic force microscopy we characterized the capacity of amyloid peptide AÎ² 42 to promote magnetite formation.