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dc.contributor.author
Celej, Maria Soledad
dc.contributor.author
Sarroukh, R.,
dc.contributor.author
Goormaghtigh, E.,
dc.contributor.author
Fidelio, Gerardo Daniel
dc.contributor.author
Ruysschaert, Jean-Marie
dc.contributor.author
Raussens, Vincent
dc.date.available
2023-05-19T14:30:08Z
dc.date.issued
2012-05
dc.identifier.citation
Celej, Maria Soledad; Sarroukh, R.,; Goormaghtigh, E.,; Fidelio, Gerardo Daniel; Ruysschaert, Jean-Marie; et al.; Toxic prefibrillar α-synuclein amyloid oligomers adopt a distinctive antiparallel β-sheet structure; Journal of the Serbian Chemical Society; Biochemical Journal; 443; 3; 5-2012; 719-726
dc.identifier.issn
0264-6021
dc.identifier.uri
http://hdl.handle.net/11336/198102
dc.description.abstract
Parkinson's disease is an age-related movement disorder characterized by the presence in the mid-brain of amyloid deposits of the 140-amino-acid protein AS (α-synuclein). AS fibrillation follows a nucleation polymerization pathway involving diverse transient prefibrillar species varying in size and morphology. Similar to other neurodegenerative diseases, cytotoxicity is currently attributed to these prefibrillar species rather than to the insoluble aggregates. Nevertheless, the underlying molecular mechanisms responsible for cytotoxicity remain elusive and structural studies may contribute to the understanding of both the amyloid aggregation mechanism and oligomer-induced toxicity. It is already recognized that soluble oligomeric AS species adopt β-sheet structures that differ from those characterizing the fibrillar structure. In the present study we used ATR (attenuated total reflection)-FTIR (Fourier-transform infrared) spectroscopy, a technique especially sensitive to β-sheet structure, to get a deeper insight into the β-sheet organization within oligomers and fibrils. Careful spectral analysis revealed that AS oligomers adopt an antiparallel β-sheet structure, whereas fibrils adopt a parallel arrangement. The results are discussed in terms of regions of the protein involved in the early β- sheet interactions and the implications of such conformational arrangement for the pathogenicity associated with AS oligomers. © The Authors Journal compilation © 2012 Biochemical Society.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Journal of the Serbian Chemical Society
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Α-SYNUCLEIN
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AMYLOID OLIGOMER
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AMYLOIDOGENESIS
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PARKINSON'S DISEASE
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SECONDARY STRUCTURE
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STRUCTURE-TOXICITY RELATIONSHIP
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Biofísica
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Ciencias Biológicas
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CIENCIAS NATURALES Y EXACTAS
dc.title
Toxic prefibrillar α-synuclein amyloid oligomers adopt a distinctive antiparallel β-sheet structure
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2023-05-18T14:39:43Z
dc.identifier.eissn
1470-8728
dc.journal.volume
443
dc.journal.number
3
dc.journal.pagination
719-726
dc.journal.pais
Reino Unido
dc.journal.ciudad
Londres
dc.description.fil
Fil: Celej, Maria Soledad. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
dc.description.fil
Fil: Sarroukh, R.,. Université Libre de Bruxelles; Bélgica
dc.description.fil
Fil: Goormaghtigh, E.,. Université Libre de Bruxelles; Bélgica
dc.description.fil
Fil: Fidelio, Gerardo Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
dc.description.fil
Fil: Ruysschaert, Jean-Marie. Université Libre de Bruxelles; Bélgica
dc.description.fil
Fil: Raussens, Vincent. Université Libre de Bruxelles; Bélgica
dc.journal.title
Biochemical Journal
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1042/BJ20111924
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://pubmed.ncbi.nlm.nih.gov/22316405/
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