Cu2 -induced modification of the kinetics of Aβ(1-42) channels

Abstract

We found that the amyloid β peptide Aβ(1-42) is capable of interacting with membrane and forming heterogeneous ion channels in the absence of any added Cu2+ or biological redox agents that have been reported to mediate Aβ(1-42) toxicity. The Aβ(1-42)-formed cation channel was inhibited by Cu2+ in cis solution ([Cu2+]cis) in a voltage- and concentration-dependent manner between 0 and 250 μM. The [Cu2+]cis-induced channel inhibition is fully reversible at low concentrations between 50 and 100 μM [Cu2+]cis and partially reversible at 250 μM [Cu2+]cis. The inhibitory effects of [Cu2+]cis between 50 and 250 μM on the channel could not be reversed with addition of Cu2+-chelating agent clioquinol (..