Richard C. Scarpa

TL;DR: It is shown that human A beta directly produces hydrogen peroxide (H2O2) by a mechanism that involves the reduction of metal ions, Fe(III) or Cu(II), setting up conditions for Fenton-type chemistry.

TL;DR: Results indicate that H+-induced conformational changes unmask a metal-binding site on Aβ that mediates reversible assembly of the peptide that explains the recently reported enrichment of these metal ions in amyloid plaques in Alzheimer's disease.

TL;DR: It is reported that Cu(II) markedly potentiates the neurotoxicity exhibited by Abeta in cell culture, suggesting that certain redox active metal ions may be important in exacerbating and perhaps facilitating Abeta-mediated oxidative damage in Alzheimer's disease.

TL;DR: A ligand displacement technique that uses metal-chelator complexes to evaluate metal ion binding to Abeta, a notoriously self-aggregating peptide, indicated that there is a very-high-affinity Cu(2+)-binding site on Abeta1-42 that mediates peptide precipitation and that the tendency of this peptide toSelf-aggregate in aqueous solutions is due to the presence of trace metal contamination.

TL;DR: The reaction of kynurenine pathway catabolites with copper and iron, as well as interactions with the major lenticular structural proteins, the alpha-crystallins, support the possibility that 3HK and 3HAA may be cofactors in the oxidative damage of proteins through interactions with redox-active metals and especially copper.