Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2051561 | FEBS Letters | 2007 | 5 Pages |
Abstract
Prions, the infectious agents responsible for the transmissible spongiform encephalopathies (TSEs) have defied full characterization for decades. Although the interactions of Cu2+ ions with PrP both in vivo and in vitro are well documented, there are still a lot of ambiguities concerning the biological and chemical nature of these effects. In this work, we have investigated the interactions of Cu2+ ions with whole repeat region of the copper-binding domain (hexapeptide repeats) of chicken PrP. Our results provide explanations for the structural and chemical basis of the specific interactions of Cu2+ ions with the hexapeptide repeat region. Furthermore, we show that SOD-like activity depends on Cu2+ complexes.
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Authors
Paweł Stańczak, Paulina Juszczyk, Zbigniew Grzonka, Henryk Kozłowski,