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dc.contributor.author
Masman, Marcelo Fabricio  
dc.contributor.author
Eisel, Ulrich L. M.  
dc.contributor.author
Csizmadia, Imre G.  
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Penke, Botond  
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Enriz, Ricardo Daniel  
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Marrink, Siewert Jan  
dc.contributor.author
Luiten, Paul G. M.  
dc.date.available
2021-04-21T12:24:54Z  
dc.date.issued
2009-11  
dc.identifier.citation
Masman, Marcelo Fabricio; Eisel, Ulrich L. M.; Csizmadia, Imre G.; Penke, Botond; Enriz, Ricardo Daniel; et al.; In Silico Study of Full-Length Amyloid 1-42 Tri- and Penta-Oligomers in Solution; American Chemical Society; Journal of Physical Chemistry B; 113; 34; 11-2009; 11710-11719  
dc.identifier.issn
1089-5647  
dc.identifier.uri
http://hdl.handle.net/11336/130591  
dc.description.abstract
Amyloid oligomers are considered to play causal roles in the pathogenesis of amyloid-related degenerative diseases including Alzheimer's disease. Using MD simulation techniques, we explored the contributions of the different structural elements of trimeric and pentameric full-length Aβ 1-42 aggregates in solution to their stability and conformational dynamics. We found that our models are stable at a temperature of 310 K, and converge toward an interdigitated side-chain packing for intermolecular contacts within the two β-sheet regions of the aggregates: β1 (residues 18-26) and β2 (residues 31-42). MD simulations reveal that the /3-strand twist is a characteristic element of Aβ-aggregates, permitting a compact, interdigitated packing of side chains from neighboring β-sheets. The β2 portion formed a tightly organized β-helix, whereas the β1 portion did not show such a firm structural organization, although it maintained its β-sheet conformation. Our simulations indicate that the hydrophobic core comprising the β2 portion of the aggregate is a crucial stabilizing element in the Aβ aggregation process. On the basis of these structure-stability findings, the β2 portion emerges as an optimal target for further antiamyloid drug design.  
dc.format
application/pdf  
dc.language.iso
eng  
dc.publisher
American Chemical Society  
dc.rights
info:eu-repo/semantics/openAccess  
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/  
dc.subject
Molecular dynamics  
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Amiloid  
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Físico-Química, Ciencia de los Polímeros, Electroquímica  
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Ciencias Químicas  
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CIENCIAS NATURALES Y EXACTAS  
dc.title
In Silico Study of Full-Length Amyloid 1-42 Tri- and Penta-Oligomers in Solution  
dc.type
info:eu-repo/semantics/article  
dc.type
info:ar-repo/semantics/artículo  
dc.type
info:eu-repo/semantics/publishedVersion  
dc.date.updated
2020-07-22T15:43:55Z  
dc.identifier.eissn
1520-6106  
dc.journal.volume
113  
dc.journal.number
34  
dc.journal.pagination
11710-11719  
dc.journal.pais
Estados Unidos  
dc.journal.ciudad
Washington  
dc.description.fil
Fil: Masman, Marcelo Fabricio. University of Groningen; Países Bajos. Universidad Nacional de San Luis; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis; Argentina  
dc.description.fil
Fil: Eisel, Ulrich L. M.. University of Groningen; Países Bajos  
dc.description.fil
Fil: Csizmadia, Imre G.. University of Toronto; Canadá. University of Szeged; Hungría  
dc.description.fil
Fil: Penke, Botond. University of Szeged; Hungría  
dc.description.fil
Fil: Enriz, Ricardo Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis. Instituto Multidisciplinario de Investigaciones Biológicas de San Luis. Universidad Nacional de San Luis. Facultad de Ciencias Físico Matemáticas y Naturales. Instituto Multidisciplinario de Investigaciones Biológicas de San Luis; Argentina  
dc.description.fil
Fil: Marrink, Siewert Jan. University of Groningen; Países Bajos  
dc.description.fil
Fil: Luiten, Paul G. M.. University of Groningen; Países Bajos  
dc.journal.title
Journal of Physical Chemistry B  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://pubs.acs.org/doi/10.1021/jp901057w  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1021/jp901057w