Metals have been shown to play a role in the genesis and development of many neurodegenerative diseases. Park9 encoded protein can protect cells from manganese poisoning, an environmental risk factor for a Parkinson’s disease- like syndrome. Park9 belongs to a family of ATP-ases involved in metal coordination and transportation; familial mutations of this gene may result in early development of PD. We tested two peptide sequences from Park9, -P1D2E3K4H5E6L7-(1) and -F1C2G3D4G5A6N7D8C9G10-(2), for Mn(II), Zn(II) and Cu(II) binding. These fragments are located from 1165 to 1171 and from 1184 to 1193 residues in Park9 sequence, and are highly conserved in a number of organisms, from yeasts to humans. Experiments have been carried out at different pH values and ligand/metal molar ratios with both potentiometric and spectroscopic (NMR, UV-vis) techniques, showing that the three metals are able to effectively bind the examined peptides. Mn(II) and Zn(II) coordination with peptide (1) involves imidazol of His5 and carboxyl γ-O of Asp2, Glu3and Glu6residues, in a distorted octahedral geometry, possibly involving bidentate interaction of carboxyl groups; four donor atoms participate in Zn(II) binding, resulting in a tetracoordinated geometry. Mn(II) and Zn(II) coordination involves the two cysteines in peptide (2); Mn(II) accepts additional ligand bonds from D4 and D8 to complete the coordination sphere, together with some water molecules. Details of Cu(II) coordination are under study.

Interaction of divalent cations with protein PARK9 / Zoroddu, Maria Antonietta; Peana, Massimiliano Francesco; Medici, Serenella; Solinas, Costantino; Juliano, Claudia Clelia Assunta; Remelli, Maurizio. - (2013), pp. 39-39. (Intervento presentato al convegno 12. International symposium on metal ions in biology and medicine: abstracts and proceedings).

Interaction of divalent cations with protein PARK9

Zoroddu, Maria Antonietta;Peana, Massimiliano Francesco;Medici, Serenella;Solinas, Costantino;Juliano, Claudia Clelia Assunta;
2013-01-01

Abstract

Metals have been shown to play a role in the genesis and development of many neurodegenerative diseases. Park9 encoded protein can protect cells from manganese poisoning, an environmental risk factor for a Parkinson’s disease- like syndrome. Park9 belongs to a family of ATP-ases involved in metal coordination and transportation; familial mutations of this gene may result in early development of PD. We tested two peptide sequences from Park9, -P1D2E3K4H5E6L7-(1) and -F1C2G3D4G5A6N7D8C9G10-(2), for Mn(II), Zn(II) and Cu(II) binding. These fragments are located from 1165 to 1171 and from 1184 to 1193 residues in Park9 sequence, and are highly conserved in a number of organisms, from yeasts to humans. Experiments have been carried out at different pH values and ligand/metal molar ratios with both potentiometric and spectroscopic (NMR, UV-vis) techniques, showing that the three metals are able to effectively bind the examined peptides. Mn(II) and Zn(II) coordination with peptide (1) involves imidazol of His5 and carboxyl γ-O of Asp2, Glu3and Glu6residues, in a distorted octahedral geometry, possibly involving bidentate interaction of carboxyl groups; four donor atoms participate in Zn(II) binding, resulting in a tetracoordinated geometry. Mn(II) and Zn(II) coordination involves the two cysteines in peptide (2); Mn(II) accepts additional ligand bonds from D4 and D8 to complete the coordination sphere, together with some water molecules. Details of Cu(II) coordination are under study.
2013
978-9974-0-0911-0
Interaction of divalent cations with protein PARK9 / Zoroddu, Maria Antonietta; Peana, Massimiliano Francesco; Medici, Serenella; Solinas, Costantino; Juliano, Claudia Clelia Assunta; Remelli, Maurizio. - (2013), pp. 39-39. (Intervento presentato al convegno 12. International symposium on metal ions in biology and medicine: abstracts and proceedings).
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11388/264686
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