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Metal-induced changes of amyloid proteins associated with neurodegenerative diseases

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Autori: Drochioiu, G., Manea, M., Murariu, M., Popa, K., Gradinaru, R., Przybylski, M

Editorial: Ph. Collery, I. Maymard, T. Theophanides, L. Khassanova, T. Collery, John Libbey Eurotext, Paris, Metal Ions in Biology and Medicine: XIII Neurology, 10, p.664-669, 2008.


The interaction between metal ions and peptides has been investigated by using mass spectrometry, atomic force microscopy, and circular dichroism techniques. Cu2+, Zn2+ and other ions bind amyloid beta peptide (Ab) to induce aggregation and form reactive oxygen species. These reactions may play a deleterious role in the disease state, because high concentrations of iron, copper, and zinc have been located in amyloid proteins in diseased brains. Here we show conformational changes of Ab peptide and its fragments in the presence of metal ions as well as the binding sites of peptide under various environmental conditions. The competitive role of various peptides for metal ions was also investigated.

Cuvinte cheie: Metal ions, amyloid beta peptide, metal-peptide complex, glutathione, mass spectrometry, atomic force microscopy, circular dichroism