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Copper Modulation of Ion Channels of PrP[106-126] Mutant Prion Peptide Fragments

Kourie, Joseph; Kenna, Bronwyn; Tew, D; Jobling, Michael F; Curtain, Cyril; Masters, Colin; Barnham, Kevin; Cappai, Roberto

Description

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]

CollectionsANU Research Publications
Date published: 2003
Type: Journal article
URI: http://hdl.handle.net/1885/75418
Source: Journal of Membrane Biology
DOI: 10.1007/s00232-002-2005-5

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