Copper Modulation of Ion Channels of PrP[106-126] Mutant Prion Peptide Fragments
We have shown previously that the protease-resistant and neurotoxic prion peptide fragment PrP[106-126] of human PrP incorporates into lipid bilayer membranes to form heterogeneous ion channels, one of which is a Cu2+-sensitive fast cation channel. To investigate the role of PrP[106-126]'s hydrophobic core, AGAAAAGA, on its ability to form ion channels and their regulation with Cu2+, we used the lipid-bilayer technique to examine membrane currents induced as a result of PrP[106-126] (AA/SS) and...[Show more]
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|Source:||Journal of Membrane Biology|
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