Interaction of Cu(II) and Ni(II) with Ypk9 Protein Fragment via NMR Studies
P1D2E3K4H5E6L7 (PK9-H), a fragment of Ypk9, the yeast homologue of the human Park9 protein, was studied for its coordination abilities towards Ni(II) and Cu(II) ions through mono- and bi-dimensional NMR techniques. Both proteins are involved in the transportation of metal ions, including manganese a...
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| Language: | English |
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Wiley
2014-01-01
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| Series: | The Scientific World Journal |
| Online Access: | http://dx.doi.org/10.1155/2014/656201 |
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| author | Massimiliano Francesco Peana Serenella Medici Alessia Ledda Valeria Marina Nurchi Maria Antonietta Zoroddu |
| author_facet | Massimiliano Francesco Peana Serenella Medici Alessia Ledda Valeria Marina Nurchi Maria Antonietta Zoroddu |
| author_sort | Massimiliano Francesco Peana |
| collection | DOAJ |
| description | P1D2E3K4H5E6L7 (PK9-H), a fragment of Ypk9, the yeast homologue of the human Park9 protein, was studied for its coordination abilities towards Ni(II) and Cu(II) ions through mono- and bi-dimensional NMR techniques. Both proteins are involved in the transportation of metal ions, including manganese and nickel, from the cytosol to the lysosomal lumen. Ypk9 showed manganese detoxification role, preventing a Mn-induced Parkinsonism (PD) besides mutations in Park9, linked to a juvenile form of the disease. Here, we tested PK9-H with Cu(II) and Ni(II) ions, the former because it is an essential element ubiquitous in the human body, so its trafficking should be strictly regulated and one cannot exclude that Ypk9 may play a role in it, and the latter because, besides being a toxic element for many organisms and involved in different pathologies and inflammation states, it seems that the protein confers protection against it. NMR experiments showed that both cations can bind PK9-H in an effective way, leading to complexes whose coordination mode depends on the pH of the solution. NMR data have been used to build a model for the structure of the major Cu(II) and Ni(II) complexes. Structural changes in the conformation of the peptide with organized side chain orientation promoted by nickel coordination were detected. |
| format | Article |
| id | doaj-art-7212df10403d40a2a3bf5a36797e3df0 |
| institution | Kabale University |
| issn | 2356-6140 1537-744X |
| language | English |
| publishDate | 2014-01-01 |
| publisher | Wiley |
| record_format | Article |
| series | The Scientific World Journal |
| spelling | doaj-art-7212df10403d40a2a3bf5a36797e3df02025-02-03T05:43:49ZengWileyThe Scientific World Journal2356-61401537-744X2014-01-01201410.1155/2014/656201656201Interaction of Cu(II) and Ni(II) with Ypk9 Protein Fragment via NMR StudiesMassimiliano Francesco Peana0Serenella Medici1Alessia Ledda2Valeria Marina Nurchi3Maria Antonietta Zoroddu4Department of Chemistry and Pharmacy, University of Sassari, Via Vienna 2, 07100 Sassari, ItalyDepartment of Chemistry and Pharmacy, University of Sassari, Via Vienna 2, 07100 Sassari, ItalyDepartment of Chemistry and Pharmacy, University of Sassari, Via Vienna 2, 07100 Sassari, ItalyDepartment of Chemical and Geological Sciences, University of Cagliari, Cittadella Universitaria, 09042 Monserrato, ItalyDepartment of Chemistry and Pharmacy, University of Sassari, Via Vienna 2, 07100 Sassari, ItalyP1D2E3K4H5E6L7 (PK9-H), a fragment of Ypk9, the yeast homologue of the human Park9 protein, was studied for its coordination abilities towards Ni(II) and Cu(II) ions through mono- and bi-dimensional NMR techniques. Both proteins are involved in the transportation of metal ions, including manganese and nickel, from the cytosol to the lysosomal lumen. Ypk9 showed manganese detoxification role, preventing a Mn-induced Parkinsonism (PD) besides mutations in Park9, linked to a juvenile form of the disease. Here, we tested PK9-H with Cu(II) and Ni(II) ions, the former because it is an essential element ubiquitous in the human body, so its trafficking should be strictly regulated and one cannot exclude that Ypk9 may play a role in it, and the latter because, besides being a toxic element for many organisms and involved in different pathologies and inflammation states, it seems that the protein confers protection against it. NMR experiments showed that both cations can bind PK9-H in an effective way, leading to complexes whose coordination mode depends on the pH of the solution. NMR data have been used to build a model for the structure of the major Cu(II) and Ni(II) complexes. Structural changes in the conformation of the peptide with organized side chain orientation promoted by nickel coordination were detected.http://dx.doi.org/10.1155/2014/656201 |
| spellingShingle | Massimiliano Francesco Peana Serenella Medici Alessia Ledda Valeria Marina Nurchi Maria Antonietta Zoroddu Interaction of Cu(II) and Ni(II) with Ypk9 Protein Fragment via NMR Studies The Scientific World Journal |
| title | Interaction of Cu(II) and Ni(II) with Ypk9 Protein Fragment via NMR Studies |
| title_full | Interaction of Cu(II) and Ni(II) with Ypk9 Protein Fragment via NMR Studies |
| title_fullStr | Interaction of Cu(II) and Ni(II) with Ypk9 Protein Fragment via NMR Studies |
| title_full_unstemmed | Interaction of Cu(II) and Ni(II) with Ypk9 Protein Fragment via NMR Studies |
| title_short | Interaction of Cu(II) and Ni(II) with Ypk9 Protein Fragment via NMR Studies |
| title_sort | interaction of cu ii and ni ii with ypk9 protein fragment via nmr studies |
| url | http://dx.doi.org/10.1155/2014/656201 |
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