Iron is an essential nutrient which is necessary for many of the biochemical processes of the body; however, it is also present in neurofibriallary tangles, glial cells and amyloid-beta (A�) plaques, which are deposits present in the brains of Alzheimer's Patients. Iron is usually carried in the blood by ferritin, an iron storage protein found in high concentrations around the A� plaques. Here we present fluorescence spectroscopy studies of the interaction of iron with the A� peptide. Iron induced changes in the tyrosine fluorescence of A�(1-16) indicate that iron binding occurs through tyrosine-10. The binding affinity of iron to A�(1-16) will be discussed along with explain the observation that iron has a possible role in stabilizing the aggregated state, but also may explain why this cation has elevated levels in senile plaques. The aim of this work is to look at the binding sites of iron to the A� peptide and define the role of iron in amyloid aggregation.

Examination of the binding of iron(III) to the amyloid-beta peptide  and its potential implications in Alzheimer's disease

243rd National Meeting (2012)

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