The whole hexapeptide repeats domain from avian PrP displays untypical hallmarks in aspect of the Cu2+ complexes formation.
Prions, the infectious agents responsible for the transmissible spongiform encephalopathies (TSEs) have defied full characterization for decades. Although the interactions of Cu(2+) 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 Cu(2+) 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 Cu(2+) ions with the hexapeptide repeat region. Furthermore, we show that SOD-like activity depends on Cu(2+) complexes.
Stańczak
Paweł
P
Faculty of Chemistry, University of Wrocław, F. Joliot-Curie 14, 50-383 Wroclaw, Poland.
Juszczyk
Paulina
P
Grzonka
Zbigniew
Z
Kozłowski
Henryk
H
D000595:Amino Acid Sequence; D000818:Animals; D002645:Chickens; D003300:Copper / Q000737:chemistry* / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D008969:Molecular Sequence Data; D011199:Potentiometry; D011328:Prions / Q000737:chemistry* / Q000378:metabolism; D017434:Protein Structure, Tertiary; D020449:Repetitive Sequences, Amino Acid; D013482:Superoxide Dismutase / Q000737:chemistry / Q000378:metabolism