ISBN: 978-83-60043-10-3 - eurobic9

Eurobic9, 2-6 September, 2008, Wrocław, Poland
P190. Interaction of Zebrafisch “Prion Related Protein” (Prp-Rel-2) with
Zn 2+ Ions
Ł. Szyrwiel a , E. Jankowska b , A. Marcinkowska b , Z. Szewczuk a , H. Kozłowski a
a Faculty of Chemistry, University of Wrocław, F. Joliot-Curie 14, 50-383 Wroclaw, Poland
b Faculty of Chemistry, University of Gdańsk, Sobieskiego 18, 80-952 Gdańsk, Poland
e-mail: lukszyr@wp.pl
Mammalian prion protein (PrP) seems to play two basic biological functions: i) transport of metal ions (Cu) and
ii) SOD-like activity. 1, 2 The very effective binding of Cu 2+ to PrP derive from the fact that protein contains an
octapeptide repeat region with 4 His residues and 2 His in the neurotoxic peptide fragment.
His are very effective binding sites by using their imidazole moieties to anchor and coordinate metal ions and the
multi-His sites are even more efficient. 2 However, the fact that the His residues are separated by seven other
amino acid residues the multi-His site in mammalian protein is only effective for Cu 2+ ions, while Zn 2+ binds
very poorly. Fish proteins which could be included into the prion family contain also His rich domains with His
residues being much closer to each other. 2 In these cases proteins were found to be very effective to bind also
Zn 2+ ions. In this work we have investigate by potentiometric, NMR and ESI method the interactions of zebrafish
protein, zPrP63-87 fragments with Zn 2+ ions showing that this protein is not only effective to bind Zn 2+ ions,
but ZnL species coexists in cooperative mode with Zn2L complex.
Aknowledgements
This work was supported by Polish Ministry of Higher Education and Science
(1 T09A 008 30 and 1 T09A 149 30).
1. Stańczak, P., Kozlowski, H., Biochem Biophys Res Commun., 2007, 1, 352: 198-202.
2. Kozłowski, H., Brown, D., Valensin G., Metalochemistry of Neurodegeneration, The Royal Society of
Chemistry 2006.
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