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Amyloid ß (Aß) and alfa synuclein (αS) share the ability to selectively bind copper ions (Cu(II) and Cu(I)). During the last decade large efforts have been directed to fully characterize Cu(II) binding domains in Aß and αS. On the other hand, the corresponding Cu(I) sites have been less considered. In this study we have analyzed Cu(I) interactions with peptides derived from Aß and αS, by means of CD and NMR spectroscopy. Beyond Cu(I), we have also used Ag(I) as a probe. By monitoring the metal induced effects on αS and Aß systems, the Cu(I)/Ag(I) binding domains have been identified. The corresponding protein structural rearrangements induced by the metal ions have been investigated as well. The Cu(I) coordination spheres are discussed with a particular emphasis to the role played by Met and His residues. [ABSTRACT FROM AUTHOR]