The mode of interaction of ataxin-3 Q36 (AT-3 Q36) with selected endogenous and exogenous metal ions, namely, Zn(2+), Cu(2+), Ni(2+), and Cd(2+), was examined. Metal-ion-induced structural changes of the protein were monitored by fluorescence as well as Fourier transform Raman spectroscopy. We found that the cations tested lead to a decrease in alpha-helical content and a concurrent increase in beta-sheet as well as undefined (beta-turn and random-coil) structures. The most evident effect was observed for copper and nickel cations. After titration with these cations, the AT3 Q36 secondary structure content (27% alpha-helices in the presence of either ion, 31 and 27% beta-sheets for Cu(2+) and Ni(2+), respectively) was similar to that observed for the aggregated form of the protein (27% alpha-helices, 36% beta-sheets). Using the 1-anilinonaphthalene-8-sulfonate hydrophobic fluorescence probe, we showed that the presence of the metal ions tested led to the formation of solvent-exposed hydrophobic patches of AT-3 Q36, and that such an effect decreased with increasing ionic radius.

Stawoska, I., Weselucha Birczynska, A., Regonesi, M., Riva, M., Tortora, P., Stochel, G. (2009). Interaction of selected divalent metal ions with human ataxin-3 Q36. JBIC, 14, 1175-1185.

Interaction of selected divalent metal ions with human ataxin-3 Q36

REGONESI, MARIA ELENA;TORTORA, PAOLO;
2009

Abstract

The mode of interaction of ataxin-3 Q36 (AT-3 Q36) with selected endogenous and exogenous metal ions, namely, Zn(2+), Cu(2+), Ni(2+), and Cd(2+), was examined. Metal-ion-induced structural changes of the protein were monitored by fluorescence as well as Fourier transform Raman spectroscopy. We found that the cations tested lead to a decrease in alpha-helical content and a concurrent increase in beta-sheet as well as undefined (beta-turn and random-coil) structures. The most evident effect was observed for copper and nickel cations. After titration with these cations, the AT3 Q36 secondary structure content (27% alpha-helices in the presence of either ion, 31 and 27% beta-sheets for Cu(2+) and Ni(2+), respectively) was similar to that observed for the aggregated form of the protein (27% alpha-helices, 36% beta-sheets). Using the 1-anilinonaphthalene-8-sulfonate hydrophobic fluorescence probe, we showed that the presence of the metal ions tested led to the formation of solvent-exposed hydrophobic patches of AT-3 Q36, and that such an effect decreased with increasing ionic radius.
Articolo in rivista - Articolo scientifico
Ataxin-3, Metal ions, Secondary structures, Fourier transform Raman
English
1175
1185
Stawoska, I., Weselucha Birczynska, A., Regonesi, M., Riva, M., Tortora, P., Stochel, G. (2009). Interaction of selected divalent metal ions with human ataxin-3 Q36. JBIC, 14, 1175-1185.
Stawoska, I; Weselucha Birczynska, A; Regonesi, M; Riva, M; Tortora, P; Stochel, G
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/10281/7999
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