The whole hexapeptide repeats domain from avian PrP displays untypical hallmarks in aspect of the Cu 2+  complexes formation | Zendy

Stańczak Paweł | Zendy; Juszczyk Paulina | Zendy; Grzonka Zbigniew | Zendy; Kozłowski Henryk | Zendy

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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.

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