Abstract
Nanoscale resolution X-ray spectromicroscopy shows the co-incubation of β-amyloid (Aβ) and iron(iii) to result in aggregate structures displaying nanoscale heterogeneity in Aβ and iron chemistry, including the formation of potentially cytotoxic Fe0.
Highlights
Disrupted iron homeostasis has been implicated in the formation of the two hallmark protein lesions of Alzheimer’s disease (AD): neurofibrillary tangles composed of hyperphosphorylated tau,[11,12,13] and amyloid plaques composed of the peptide β-amyloid (Aβ).[13,14,15]
scanning transmission X-ray microscopy (STXM) speciation mapping performed at the carbon K-edge to observe peptide distribution, showed peptide structure to closely resemble the aggregates observed under transmission electron microscopy (TEM) (Fig. 1a and 2b), confirming
These results demonstrate a heterogeneity in iron loading between Aβ aggregates formed under the same starting experimental conditions
Summary
The transition metal iron is vital for healthy brain function, acting as a co-factor in numerous brain processes.[1,2,3,4] The maintenance of brain iron homeostasis is fundamental to its well-being, and multiple complex mechanisms exist to maintain this balance.[1,4] essential, iron can convey neurotoxic effects when mishandled in the brain.[4,5,6] Reactive labile iron can partake in Fenton redox chemistry, producing reactive oxygen species (ROS) capable of inducing oxidative stress, and cell death.[5,6,7] Chemically-reduced, low-oxidationstate iron (
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