Premium
The whole hexapeptide repeats domain from avian PrP displays untypical hallmarks in aspect of the Cu 2+ complexes formation
Author(s) -
Stańczak Paweł,
Juszczyk Paulina,
Grzonka Zbigniew,
Kozłowski Henryk
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.08.043
Subject(s) - in vitro , ion , in vivo , chemistry , prion protein , biophysics , copper , crystallography , biology , biochemistry , genetics , medicine , organic chemistry , disease , pathology
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.