Aβ-Amyloid fibrils are self-triggered by the interfacial lipid environment and low peptide content

Autores
Bolaño Alvarez, Alain; Caruso, Benjamin; Rodriguez, Pablo Eduardo Andres; Petersen, Steffen B.; Fidelio, Gerardo Daniel
Año de publicación
2020
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
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.
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
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
Fil: Rodriguez, Pablo Eduardo Andres. Provincia de Córdoba. Ministerio de Ciencia y Técnica; Argentina
Fil: Petersen, Steffen B.. Aalborg University; Dinamarca
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
Materia
Beta-amyloid
Fibrillogenesis
Monolayer
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/125078
Acceder
id CONICETDig_f39aeba8811243f19cde691f58208b05
oai_identifier_str oai:ri.conicet.gov.ar:11336/125078
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Aβ-Amyloid fibrils are self-triggered by the interfacial lipid environment and low peptide contentBolaño Alvarez, AlainCaruso, BenjaminRodriguez, Pablo Eduardo AndresPetersen, Steffen B.Fidelio, Gerardo DanielBeta-amyloidFibrillogenesisMonolayerhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1We 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.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; ArgentinaFil: 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; ArgentinaFil: Rodriguez, Pablo Eduardo Andres. Provincia de Córdoba. Ministerio de Ciencia y Técnica; ArgentinaFil: Petersen, Steffen B.. Aalborg University; DinamarcaFil: 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; ArgentinaAmerican Chemical Society2020-07-21info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/125078Bolaño 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; 8056-80650743-74631520-5827CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/ 10.1021/acs.langmuir.0c00468info:eu-repo/semantics/altIdentifier/url/https://pubs.acs.org/doi/pdf/10.1021/acs.langmuir.0c00468info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:47:51Zoai:ri.conicet.gov.ar:11336/125078instacron: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:34982025-09-03 09:47:51.687CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Aβ-Amyloid fibrils are self-triggered by the interfacial lipid environment and low peptide content
title Aβ-Amyloid fibrils are self-triggered by the interfacial lipid environment and low peptide content
spellingShingle Aβ-Amyloid fibrils are self-triggered by the interfacial lipid environment and low peptide content
Bolaño Alvarez, Alain
Beta-amyloid
Fibrillogenesis
Monolayer
title_short Aβ-Amyloid fibrils are self-triggered by the interfacial lipid environment and low peptide content
title_full Aβ-Amyloid fibrils are self-triggered by the interfacial lipid environment and low peptide content
title_fullStr Aβ-Amyloid fibrils are self-triggered by the interfacial lipid environment and low peptide content
title_full_unstemmed Aβ-Amyloid fibrils are self-triggered by the interfacial lipid environment and low peptide content
title_sort Aβ-Amyloid fibrils are self-triggered by the interfacial lipid environment and low peptide content
dc.creator.none.fl_str_mv Bolaño Alvarez, Alain
Caruso, Benjamin
Rodriguez, Pablo Eduardo Andres
Petersen, Steffen B.
Fidelio, Gerardo Daniel
author Bolaño Alvarez, Alain
author_facet Bolaño Alvarez, Alain
Caruso, Benjamin
Rodriguez, Pablo Eduardo Andres
Petersen, Steffen B.
Fidelio, Gerardo Daniel
author_role author
author2 Caruso, Benjamin
Rodriguez, Pablo Eduardo Andres
Petersen, Steffen B.
Fidelio, Gerardo Daniel
author2_role author
author
author
author
dc.subject.none.fl_str_mv Beta-amyloid
Fibrillogenesis
Monolayer
topic Beta-amyloid
Fibrillogenesis
Monolayer
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv 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.
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
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
Fil: Rodriguez, Pablo Eduardo Andres. Provincia de Córdoba. Ministerio de Ciencia y Técnica; Argentina
Fil: Petersen, Steffen B.. Aalborg University; Dinamarca
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
description 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.
publishDate 2020
dc.date.none.fl_str_mv 2020-07-21
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/125078
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
0743-7463
1520-5827
CONICET Digital
CONICET
url http://hdl.handle.net/11336/125078
identifier_str_mv 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
0743-7463
1520-5827
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/ 10.1021/acs.langmuir.0c00468
info:eu-repo/semantics/altIdentifier/url/https://pubs.acs.org/doi/pdf/10.1021/acs.langmuir.0c00468
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv American Chemical Society
publisher.none.fl_str_mv American Chemical Society
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
_version_ 1842268885976350720
score 13.13397

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