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It is characterized by the accumulation of amyloid\u2010<jats:italic>\u03b2<\/jats:italic> peptide (ABP) into amyloid plaques between nerve cells, which produces a massive local neurodegeneration. Molecular magnetic resonance imaging allows diagnosis of AD by showing ABP accumulation in the brain. The ultrasmall particles of iron oxide (USPIO) derivatives proposed in the present work were functionalized with peptides that present an affinity for ABP, independently of its state of aggregation. Their nanomolar <jats:italic>K<\/jats:italic><jats:sub>d<\/jats:sub>* confirms the high affinity of our vectorized contrast agents (VCA) for ABP and therefore their high labeling potential, specificity and sensitivity. Their lack of toxicity has been demonstrated, both by <jats:italic>in vitro<\/jats:italic> studies using the MTT method on several cell types, and by <jats:italic>in vivo<\/jats:italic> investigations with assessment of renal and hepatic biomarkers and by histopathology evaluation. The results of biodistribution studies corroborated by MRI demonstrate that USPIO\u2010PHO (USPIO coupled to peptide C\u2010IPLPFYN\u2010C) are able to cross the blood\u2013brain barrier without any facilitating strategy, and accumulates in the brain 90\u2009min after its injection in NMRI mice. None of the USPIO derivatives were found in any organs one week after administration. To conclude, USPIO\u2010PHO seems to have a genuine potential for labeling amyloid plaques in the brain; it has a nanomolar binding affinity, no toxic effects, and its elimination half\u2010life is about 3\u2009h. Further tests will be made on transgenic mice, aimed at confirming the potential of early AD diagnosis using our VCA. 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