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dc.contributor.author
Bolaño Alvarez, Alain  
dc.contributor.author
Caruso, Benjamin  
dc.contributor.author
Rodriguez, Pablo Eduardo Andres  
dc.contributor.author
Petersen, Steffen B.  
dc.contributor.author
Fidelio, Gerardo Daniel  
dc.date.available
2021-02-08T13:45:14Z  
dc.date.issued
2020-07-21  
dc.identifier.citation
Bolaño Alvarez, Alain; Caruso, Benjamin; Rodriguez, Pablo Eduardo Andres; Petersen, Steffen B.; Fidelio, Gerardo Daniel; Aβ-Amyloid fibrils are self-triggered by the interfacial lipid environment and low peptide content; American Chemical Society; Langmuir; 36; 28; 21-7-2020; 8056-8065  
dc.identifier.issn
0743-7463  
dc.identifier.uri
http://hdl.handle.net/11336/125078  
dc.description.abstract
We studied the surface properties of Aβ(1-40) amyloid peptides mixed with 1-palmitoyl-2-oleoyl-phosphatidylcholine (POPC) (liquid state) or 1,2-disteraoyl-phosphatidylcholine (DSPC) (solid state) phospholipids by using nanostructured lipid/peptide films (Langmuir monolayers). Pure Aβ(1-40) amyloid peptides form insoluble monolayers without forming fibril-like structures. In a lipid environment [phospholipid/Aβ(1-40) peptide mixtures], we observed that both miscibility and stability of the films depend on the peptide content. At low Aβ(1-40) amyloid peptide proportion (from 2.5 to 10% of peptide area proportion), we observed the formation of a fibril-like structure when mixed only with POPC lipids. The stability acquired by these mixed films is within 20-35 mN·m-1 compatible with the equivalent surface pressure postulated for natural biomembranes. Fibrils are clearly evidenced directly from the monolayers by using Brewster angle microscopy. The so-called nanostructured fibrils are thioflavin T positive when observed by fluorescence microscopy. The amyloid fibril network at the surface was also evidenced by atomic force microscopy when the films are transferred onto a mica support. Aβ(1-40) amyloid mixed with the solid DSPC lipid showed an immiscible behavior in all peptide proportions without fibril formation. We postulated that the amyloid fibrillogenesis at the membrane can be dynamically nano-self-triggered at the surface by the quality of the interfacial environment, that is, the physical state of the water-lipid interface and the relative content of amyloid protein present at the interface.  
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
Beta-amyloid  
dc.subject
Fibrillogenesis  
dc.subject
Monolayer  
dc.subject.classification
Biofísica  
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Ciencias Biológicas  
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CIENCIAS NATURALES Y EXACTAS  
dc.title
Aβ-Amyloid fibrils are self-triggered by the interfacial lipid environment and low peptide content  
dc.type
info:eu-repo/semantics/article  
dc.type
info:ar-repo/semantics/artículo  
dc.type
info:eu-repo/semantics/publishedVersion  
dc.date.updated
2021-01-18T15:46:50Z  
dc.identifier.eissn
1520-5827  
dc.journal.volume
36  
dc.journal.number
28  
dc.journal.pagination
8056-8065  
dc.journal.pais
Estados Unidos  
dc.journal.ciudad
Washington  
dc.description.fil
Fil: Bolaño Alvarez, Alain. 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: Caruso, Benjamin. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones Biológicas y Tecnológicas. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas, Físicas y Naturales. Instituto de Investigaciones Biológicas y Tecnológicas; Argentina. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas, Físicas y Naturales. Departamento de Química. Cátedra de Química Biológica; Argentina  
dc.description.fil
Fil: Rodriguez, Pablo Eduardo Andres. Provincia de Córdoba. Ministerio de Ciencia y Técnica; Argentina  
dc.description.fil
Fil: Petersen, Steffen B.. Aalborg University; Dinamarca  
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.journal.title
Langmuir  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/ 10.1021/acs.langmuir.0c00468  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://pubs.acs.org/doi/pdf/10.1021/acs.langmuir.0c00468