A β-amino acid modified heptapeptide containing a designed recognition element disrupts fibrillization of the amyloid β-peptide

Autores
Castelletto, Valeria; Hamley, Iam W.; Lim, Teck; de Tullio, Matias Blas; Castaño, Eduardo Miguel
Año de publicación
2010
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
We study the complex formation of a peptide betaAbetaAKLVFF, previously developed by our group, with Abeta(1-42) in aqueous solution. Circular dichroism spectroscopy is used to probe the interactions between betaAbetaAKLVFF and Abeta(1-42), and to study the secondary structure of the species in solution. Thioflavin T fluorescence spectroscopy shows that the population of fibers is higher in betaAbetaAKLVFF/Abeta(1-42) mixtures compared to pure Abeta(1-42) solutions. TEM and cryo-TEM demonstrate that co-incubation of betaAbetaAKLVFF with Abeta(1-42) causes the formation of extended dense networks of branched fibrils, very different from the straight fibrils observed for Abeta(1-42) alone. Neurotoxicity assays show that although betaAbetaAKLVFF alters the fibrillization of Abeta(1-42), it does not decrease the neurotoxicity, which suggests that toxic oligomeric Abeta(1-42) species are still present in the betaAbetaAKLVFF/Abeta(1-42) mixtures. Our results show that our designed peptide binds to Abeta(1-42) and changes the amyloid fibril morphology. This is shown to not necessarily translate into reduced toxicity.
Fil: Castelletto, Valeria. University of Reading. Department of Chemistry; Reino Unido
Fil: Hamley, Iam W.. University of Reading. Department of Chemistry; Reino Unido. Diamond Light Source; Reino Unido
Fil: Lim, Teck. University of Oxford. Department of Materials; Reino Unido
Fil: de Tullio, Matias Blas. Fundación Instituto Leloir; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina
Fil: Castaño, Eduardo Miguel. Fundación Instituto Leloir; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina
Materia
Peptido Amiloide
Neurotoxisidad
Enfermedad Alzheimer
Modelo Celular
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:11336/12694
Acceder
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network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling A β-amino acid modified heptapeptide containing a designed recognition element disrupts fibrillization of the amyloid β-peptideCastelletto, ValeriaHamley, Iam W.Lim, Teckde Tullio, Matias BlasCastaño, Eduardo MiguelPeptido AmiloideNeurotoxisidadEnfermedad AlzheimerModelo Celularhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1We study the complex formation of a peptide betaAbetaAKLVFF, previously developed by our group, with Abeta(1-42) in aqueous solution. Circular dichroism spectroscopy is used to probe the interactions between betaAbetaAKLVFF and Abeta(1-42), and to study the secondary structure of the species in solution. Thioflavin T fluorescence spectroscopy shows that the population of fibers is higher in betaAbetaAKLVFF/Abeta(1-42) mixtures compared to pure Abeta(1-42) solutions. TEM and cryo-TEM demonstrate that co-incubation of betaAbetaAKLVFF with Abeta(1-42) causes the formation of extended dense networks of branched fibrils, very different from the straight fibrils observed for Abeta(1-42) alone. Neurotoxicity assays show that although betaAbetaAKLVFF alters the fibrillization of Abeta(1-42), it does not decrease the neurotoxicity, which suggests that toxic oligomeric Abeta(1-42) species are still present in the betaAbetaAKLVFF/Abeta(1-42) mixtures. Our results show that our designed peptide binds to Abeta(1-42) and changes the amyloid fibril morphology. This is shown to not necessarily translate into reduced toxicity.Fil: Castelletto, Valeria. University of Reading. Department of Chemistry; Reino UnidoFil: Hamley, Iam W.. University of Reading. Department of Chemistry; Reino Unido. Diamond Light Source; Reino UnidoFil: Lim, Teck. University of Oxford. Department of Materials; Reino UnidoFil: de Tullio, Matias Blas. Fundación Instituto Leloir; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; ArgentinaFil: Castaño, Eduardo Miguel. Fundación Instituto Leloir; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; ArgentinaWiley2010-09info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/12694Castelletto, Valeria; Hamley, Iam W.; Lim, Teck; de Tullio, Matias Blas; Castaño, Eduardo Miguel; A β-amino acid modified heptapeptide containing a designed recognition element disrupts fibrillization of the amyloid β-peptide; Wiley; Journal Of Peptide Science; 16; 9; 9-2010; 443-4501075-2617enginfo:eu-repo/semantics/altIdentifier/url/http://onlinelibrary.wiley.com/doi/10.1002/psc.1271/abstractinfo:eu-repo/semantics/altIdentifier/url/http://dx.doi.org/10.1002/psc.1271info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T10:11:41Zoai:ri.conicet.gov.ar:11336/12694instacron: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 10:11:42.207CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv A β-amino acid modified heptapeptide containing a designed recognition element disrupts fibrillization of the amyloid β-peptide
title A β-amino acid modified heptapeptide containing a designed recognition element disrupts fibrillization of the amyloid β-peptide
spellingShingle A β-amino acid modified heptapeptide containing a designed recognition element disrupts fibrillization of the amyloid β-peptide
Castelletto, Valeria
Peptido Amiloide
Neurotoxisidad
Enfermedad Alzheimer
Modelo Celular
title_short A β-amino acid modified heptapeptide containing a designed recognition element disrupts fibrillization of the amyloid β-peptide
title_full A β-amino acid modified heptapeptide containing a designed recognition element disrupts fibrillization of the amyloid β-peptide
title_fullStr A β-amino acid modified heptapeptide containing a designed recognition element disrupts fibrillization of the amyloid β-peptide
title_full_unstemmed A β-amino acid modified heptapeptide containing a designed recognition element disrupts fibrillization of the amyloid β-peptide
title_sort A β-amino acid modified heptapeptide containing a designed recognition element disrupts fibrillization of the amyloid β-peptide
dc.creator.none.fl_str_mv Castelletto, Valeria
Hamley, Iam W.
Lim, Teck
de Tullio, Matias Blas
Castaño, Eduardo Miguel
author Castelletto, Valeria
author_facet Castelletto, Valeria
Hamley, Iam W.
Lim, Teck
de Tullio, Matias Blas
Castaño, Eduardo Miguel
author_role author
author2 Hamley, Iam W.
Lim, Teck
de Tullio, Matias Blas
Castaño, Eduardo Miguel
author2_role author
author
author
author
dc.subject.none.fl_str_mv Peptido Amiloide
Neurotoxisidad
Enfermedad Alzheimer
Modelo Celular
topic Peptido Amiloide
Neurotoxisidad
Enfermedad Alzheimer
Modelo Celular
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 study the complex formation of a peptide betaAbetaAKLVFF, previously developed by our group, with Abeta(1-42) in aqueous solution. Circular dichroism spectroscopy is used to probe the interactions between betaAbetaAKLVFF and Abeta(1-42), and to study the secondary structure of the species in solution. Thioflavin T fluorescence spectroscopy shows that the population of fibers is higher in betaAbetaAKLVFF/Abeta(1-42) mixtures compared to pure Abeta(1-42) solutions. TEM and cryo-TEM demonstrate that co-incubation of betaAbetaAKLVFF with Abeta(1-42) causes the formation of extended dense networks of branched fibrils, very different from the straight fibrils observed for Abeta(1-42) alone. Neurotoxicity assays show that although betaAbetaAKLVFF alters the fibrillization of Abeta(1-42), it does not decrease the neurotoxicity, which suggests that toxic oligomeric Abeta(1-42) species are still present in the betaAbetaAKLVFF/Abeta(1-42) mixtures. Our results show that our designed peptide binds to Abeta(1-42) and changes the amyloid fibril morphology. This is shown to not necessarily translate into reduced toxicity.
Fil: Castelletto, Valeria. University of Reading. Department of Chemistry; Reino Unido
Fil: Hamley, Iam W.. University of Reading. Department of Chemistry; Reino Unido. Diamond Light Source; Reino Unido
Fil: Lim, Teck. University of Oxford. Department of Materials; Reino Unido
Fil: de Tullio, Matias Blas. Fundación Instituto Leloir; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina
Fil: Castaño, Eduardo Miguel. Fundación Instituto Leloir; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina
description We study the complex formation of a peptide betaAbetaAKLVFF, previously developed by our group, with Abeta(1-42) in aqueous solution. Circular dichroism spectroscopy is used to probe the interactions between betaAbetaAKLVFF and Abeta(1-42), and to study the secondary structure of the species in solution. Thioflavin T fluorescence spectroscopy shows that the population of fibers is higher in betaAbetaAKLVFF/Abeta(1-42) mixtures compared to pure Abeta(1-42) solutions. TEM and cryo-TEM demonstrate that co-incubation of betaAbetaAKLVFF with Abeta(1-42) causes the formation of extended dense networks of branched fibrils, very different from the straight fibrils observed for Abeta(1-42) alone. Neurotoxicity assays show that although betaAbetaAKLVFF alters the fibrillization of Abeta(1-42), it does not decrease the neurotoxicity, which suggests that toxic oligomeric Abeta(1-42) species are still present in the betaAbetaAKLVFF/Abeta(1-42) mixtures. Our results show that our designed peptide binds to Abeta(1-42) and changes the amyloid fibril morphology. This is shown to not necessarily translate into reduced toxicity.
publishDate 2010
dc.date.none.fl_str_mv 2010-09
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/11336/12694
Castelletto, Valeria; Hamley, Iam W.; Lim, Teck; de Tullio, Matias Blas; Castaño, Eduardo Miguel; A β-amino acid modified heptapeptide containing a designed recognition element disrupts fibrillization of the amyloid β-peptide; Wiley; Journal Of Peptide Science; 16; 9; 9-2010; 443-450
1075-2617
url http://hdl.handle.net/11336/12694
identifier_str_mv Castelletto, Valeria; Hamley, Iam W.; Lim, Teck; de Tullio, Matias Blas; Castaño, Eduardo Miguel; A β-amino acid modified heptapeptide containing a designed recognition element disrupts fibrillization of the amyloid β-peptide; Wiley; Journal Of Peptide Science; 16; 9; 9-2010; 443-450
1075-2617
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://onlinelibrary.wiley.com/doi/10.1002/psc.1271/abstract
info:eu-repo/semantics/altIdentifier/url/http://dx.doi.org/10.1002/psc.1271
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 Wiley
publisher.none.fl_str_mv Wiley
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
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score 13.13397

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