Exploring the Structural Details of Cu(I) Binding to α-Synuclein by NMR Spectroscopy
- Autores
- Binolfi, Andrés; Valiente Gabioud, Ariel Alejandro; Duran, Rosario; Zweckstetter, Markus; Griesinger, Christian; Fernandez, Claudio Oscar
- Año de publicación
- 2010
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- The aggregation of α-synuclein (AS) is selectively enhanced by copper in vitro, and the interaction is proposed to play a potential role in vivo. In this work, we report the structural, residue-specific characterization of Cu(I) binding to AS and demonstrate that the protein is able to bind Cu(I) with relatively high affinity in a coordination environment that involves the participation of Met1 and Met5 residues. This knowledge is a key to understanding the structural-aggregation basis of the copper-catalyzed oxidation of AS.
Fil: Binolfi, Andrés. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Valiente Gabioud, Ariel Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Duran, Rosario. Instituto Pasteur de Montevideo; Uruguay. Instituto de Investigaciones Biológicas "Clemente Estable"; Uruguay
Fil: Zweckstetter, Markus. Research Center for the Molecular Physiology of the Brain; Alemania. Max Planck Institute for Biophysical Chemistry; Alemania
Fil: Griesinger, Christian. Research Center for the Molecular Physiology of the Brain; Alemania
Fil: Fernandez, Claudio Oscar. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina. Research Center for the Molecular Physiology of the Brain; Alemania - Materia
-
Amyloid
NMR spectroscopy
Metal catalyzed oxidation
Nuerodegeneration - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
- Repositorio
.jpg)
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/278367
Ver los metadatos del registro completo
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Exploring the Structural Details of Cu(I) Binding to α-Synuclein by NMR SpectroscopyBinolfi, AndrésValiente Gabioud, Ariel AlejandroDuran, RosarioZweckstetter, MarkusGriesinger, ChristianFernandez, Claudio OscarAmyloidNMR spectroscopyMetal catalyzed oxidationNuerodegenerationhttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1The aggregation of α-synuclein (AS) is selectively enhanced by copper in vitro, and the interaction is proposed to play a potential role in vivo. In this work, we report the structural, residue-specific characterization of Cu(I) binding to AS and demonstrate that the protein is able to bind Cu(I) with relatively high affinity in a coordination environment that involves the participation of Met1 and Met5 residues. This knowledge is a key to understanding the structural-aggregation basis of the copper-catalyzed oxidation of AS.Fil: Binolfi, Andrés. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; ArgentinaFil: Valiente Gabioud, Ariel Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; ArgentinaFil: Duran, Rosario. Instituto Pasteur de Montevideo; Uruguay. Instituto de Investigaciones Biológicas "Clemente Estable"; UruguayFil: Zweckstetter, Markus. Research Center for the Molecular Physiology of the Brain; Alemania. Max Planck Institute for Biophysical Chemistry; AlemaniaFil: Griesinger, Christian. Research Center for the Molecular Physiology of the Brain; AlemaniaFil: Fernandez, Claudio Oscar. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina. Research Center for the Molecular Physiology of the Brain; AlemaniaAmerican Chemical Society2010-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/278367Binolfi, Andrés; Valiente Gabioud, Ariel Alejandro; Duran, Rosario; Zweckstetter, Markus; Griesinger, Christian; et al.; Exploring the Structural Details of Cu(I) Binding to α-Synuclein by NMR Spectroscopy; American Chemical Society; Journal of the American Chemical Society; 133; 2; 12-2010; 194-1960002-7863CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://pubs.acs.org/doi/10.1021/ja107842finfo:eu-repo/semantics/altIdentifier/doi/10.1021/ja107842finfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2026-01-08T13:05:50Zoai:ri.conicet.gov.ar:11336/278367instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982026-01-08 13:05:51.087CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
| dc.title.none.fl_str_mv |
Exploring the Structural Details of Cu(I) Binding to α-Synuclein by NMR Spectroscopy |
| title |
Exploring the Structural Details of Cu(I) Binding to α-Synuclein by NMR Spectroscopy |
| spellingShingle |
Exploring the Structural Details of Cu(I) Binding to α-Synuclein by NMR Spectroscopy Binolfi, Andrés Amyloid NMR spectroscopy Metal catalyzed oxidation Nuerodegeneration |
| title_short |
Exploring the Structural Details of Cu(I) Binding to α-Synuclein by NMR Spectroscopy |
| title_full |
Exploring the Structural Details of Cu(I) Binding to α-Synuclein by NMR Spectroscopy |
| title_fullStr |
Exploring the Structural Details of Cu(I) Binding to α-Synuclein by NMR Spectroscopy |
| title_full_unstemmed |
Exploring the Structural Details of Cu(I) Binding to α-Synuclein by NMR Spectroscopy |
| title_sort |
Exploring the Structural Details of Cu(I) Binding to α-Synuclein by NMR Spectroscopy |
| dc.creator.none.fl_str_mv |
Binolfi, Andrés Valiente Gabioud, Ariel Alejandro Duran, Rosario Zweckstetter, Markus Griesinger, Christian Fernandez, Claudio Oscar |
| author |
Binolfi, Andrés |
| author_facet |
Binolfi, Andrés Valiente Gabioud, Ariel Alejandro Duran, Rosario Zweckstetter, Markus Griesinger, Christian Fernandez, Claudio Oscar |
| author_role |
author |
| author2 |
Valiente Gabioud, Ariel Alejandro Duran, Rosario Zweckstetter, Markus Griesinger, Christian Fernandez, Claudio Oscar |
| author2_role |
author author author author author |
| dc.subject.none.fl_str_mv |
Amyloid NMR spectroscopy Metal catalyzed oxidation Nuerodegeneration |
| topic |
Amyloid NMR spectroscopy Metal catalyzed oxidation Nuerodegeneration |
| purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.4 https://purl.org/becyt/ford/1 |
| dc.description.none.fl_txt_mv |
The aggregation of α-synuclein (AS) is selectively enhanced by copper in vitro, and the interaction is proposed to play a potential role in vivo. In this work, we report the structural, residue-specific characterization of Cu(I) binding to AS and demonstrate that the protein is able to bind Cu(I) with relatively high affinity in a coordination environment that involves the participation of Met1 and Met5 residues. This knowledge is a key to understanding the structural-aggregation basis of the copper-catalyzed oxidation of AS. Fil: Binolfi, Andrés. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina Fil: Valiente Gabioud, Ariel Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina Fil: Duran, Rosario. Instituto Pasteur de Montevideo; Uruguay. Instituto de Investigaciones Biológicas "Clemente Estable"; Uruguay Fil: Zweckstetter, Markus. Research Center for the Molecular Physiology of the Brain; Alemania. Max Planck Institute for Biophysical Chemistry; Alemania Fil: Griesinger, Christian. Research Center for the Molecular Physiology of the Brain; Alemania Fil: Fernandez, Claudio Oscar. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina. Research Center for the Molecular Physiology of the Brain; Alemania |
| description |
The aggregation of α-synuclein (AS) is selectively enhanced by copper in vitro, and the interaction is proposed to play a potential role in vivo. In this work, we report the structural, residue-specific characterization of Cu(I) binding to AS and demonstrate that the protein is able to bind Cu(I) with relatively high affinity in a coordination environment that involves the participation of Met1 and Met5 residues. This knowledge is a key to understanding the structural-aggregation basis of the copper-catalyzed oxidation of AS. |
| publishDate |
2010 |
| dc.date.none.fl_str_mv |
2010-12 |
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info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion http://purl.org/coar/resource_type/c_6501 info:ar-repo/semantics/articulo |
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article |
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publishedVersion |
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http://hdl.handle.net/11336/278367 Binolfi, Andrés; Valiente Gabioud, Ariel Alejandro; Duran, Rosario; Zweckstetter, Markus; Griesinger, Christian; et al.; Exploring the Structural Details of Cu(I) Binding to α-Synuclein by NMR Spectroscopy; American Chemical Society; Journal of the American Chemical Society; 133; 2; 12-2010; 194-196 0002-7863 CONICET Digital CONICET |
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http://hdl.handle.net/11336/278367 |
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Binolfi, Andrés; Valiente Gabioud, Ariel Alejandro; Duran, Rosario; Zweckstetter, Markus; Griesinger, Christian; et al.; Exploring the Structural Details of Cu(I) Binding to α-Synuclein by NMR Spectroscopy; American Chemical Society; Journal of the American Chemical Society; 133; 2; 12-2010; 194-196 0002-7863 CONICET Digital CONICET |
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eng |
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eng |
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American Chemical Society |
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American Chemical Society |
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CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas |
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