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

Eurobic9, 2-6 September, 2008, Wrocław, Poland
O8. Comparison of the Metal Binding Affinities of Prion and Amyloid
Peptide Fragments
I. Sóvágó
Inorganic and Analytical Chemistry, University of Debrecen, Egyetem ter 1., 4010, DEBRECEN, Hungary
e-mail: sovago@delfin.unideb.hu
The proteins responsible for the development of various forms of neurodegenerative disorders are generally rich
in histidyl residues. In the case of human prion protein six histidines are located in the disordered region of the
protein and they are well separated from each other. The hexadecapeptide Aβ(1-16) is generally considered as
the metal binding domain of amyloid peptides and it consists of three histidyl moieties; two of them are in
adjacent while the third one is located in distant positions. The presence of aspartyl and glutamyl residues
represents another important difference in the amino acid sequences of prion and amyloid fragments.
In the past few years we performed potentiometric and spectroscopic studies on the copper(II) and zinc(II)
complexes of a series of peptide fragments of prion and amyloid-β [1-3]. The results revealed that the metal
binding affinities of the peptides are largely affected by the number and location of histidyl residues. It was
found that both prion and amyloid fragments can form stable mono- and oligo-nuclear complexes with
copper(II), while zinc(II) binding affinity of amyloid peptides is much higher than those of the prion fragments.
Acknowledgements: This work was supported by the Hungarian Scientific Research Fund, OTKA T 048352.
References:
[1] G. Di Natale, G. Grasso, G. Impellizzeri, D. La Mendola, G. Micera, N. Mihala, Z. Nagy, K Ősz, G.
Pappalardo, V. Rigó, E. Razzarelli, D. Sanna, I. Sóvágó, Inorg. Chem., 2005, 44, 7214-7225.
[2] V. Jószai, Z. Nagy, K. Ősz, D. Sanna, G. Di Natale, D. La Mendola, G. Pappalardo, E. Rizzarelli and I.
Sóvágó, J. Inorg. Biochem., 2006, 100, 1399-1409.
[3] K. Ősz, Z. Nagy, G. Pappalardo, G. Di Natale, D. Sanna, G. Micera, E. Rizzarelli, I. Sóvágó: Chem. Eur. J.,
2007, 13, 7129-7143.
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