Self-assembly and anti-amyloid cytotoxicity activity of amyloid beta peptide derivatives

Autores
Castelletto, V.; Ryumin, P.; Cramer, R.; Hamley, I.W.; Taylor, M.; Allsop, D.; Reza, M.; Ruokolainen, J.; Arnold, T.; Hermida Merino, D.; Garcia, Corina Ileana; Leal, Maria Celeste; Castaño, Eduardo Miguel
Año de publicación
2017
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The self-assembly of two derivatives of KLVFF, a fragment Aβ(16-20) of the amyloid beta (Aβ) peptide, is investigated and recovery of viability of neuroblastoma cells exposed to Aβ (1-42) is observed at sub-stoichiometric peptide concentrations. Fluorescence assays show that NH 2 -KLVFF-CONH 2 undergoes hydrophobic collapse and amyloid formation at the same critical aggregation concentration (cac). In contrast, NH 2 -K(Boc)LVFF-CONH 2 undergoes hydrophobic collapse at a low concentration, followed by amyloid formation at a higher cac. These findings are supported by the β-sheet features observed by FTIR. Electrospray ionization mass spectrometry indicates that NH 2 -K(Boc)LVFF-CONH 2 forms a significant population of oligomeric species above the cac. Cryo-TEM, used together with SAXS to determine fibril dimensions, shows that the length and degree of twisting of peptide fibrils seem to be influenced by the net peptide charge. Grazing incidence X-ray scattering from thin peptide films shows features of β-sheet ordering for both peptides, along with evidence for lamellar ordering of NH 2 -KLVFF-CONH 2. This work provides a comprehensive picture of the aggregation properties of these two KLVFF derivatives and shows their utility, in unaggregated form, in restoring the viability of neuroblastoma cells against Aβ-induced toxicity.
Fil: Castelletto, V.. University of Reading; Reino Unido
Fil: Ryumin, P.. University of Reading; Reino Unido
Fil: Cramer, R.. University of Reading; Reino Unido
Fil: Hamley, I.W.. University of Reading; Reino Unido
Fil: Taylor, M.. University of Lancaster; Reino Unido
Fil: Allsop, D.. University of Lancaster; Reino Unido
Fil: Reza, M.. Aalto University; Finlandia
Fil: Ruokolainen, J.. Aalto University; Finlandia
Fil: Arnold, T.. Diamond Light Source Ltd.,Harwell Science and Innovation Campus; Reino Unido
Fil: Hermida Merino, D.. European Synchrotron Radiation Facility; Francia
Fil: Garcia, Corina Ileana. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
Fil: Leal, Maria Celeste. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
Fil: Castaño, Eduardo Miguel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
Materia
Alzheimer Diseade
Amyloid Beta
Neurodegeneration
Amyloid Beta
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:11336/92942
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/92942
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Self-assembly and anti-amyloid cytotoxicity activity of amyloid beta peptide derivativesCastelletto, V.Ryumin, P.Cramer, R.Hamley, I.W.Taylor, M.Allsop, D.Reza, M.Ruokolainen, J.Arnold, T.Hermida Merino, D.Garcia, Corina IleanaLeal, Maria CelesteCastaño, Eduardo MiguelAlzheimer DiseadeAmyloid BetaNeurodegenerationAmyloid Betahttps://purl.org/becyt/ford/3.1https://purl.org/becyt/ford/3The self-assembly of two derivatives of KLVFF, a fragment Aβ(16-20) of the amyloid beta (Aβ) peptide, is investigated and recovery of viability of neuroblastoma cells exposed to Aβ (1-42) is observed at sub-stoichiometric peptide concentrations. Fluorescence assays show that NH 2 -KLVFF-CONH 2 undergoes hydrophobic collapse and amyloid formation at the same critical aggregation concentration (cac). In contrast, NH 2 -K(Boc)LVFF-CONH 2 undergoes hydrophobic collapse at a low concentration, followed by amyloid formation at a higher cac. These findings are supported by the β-sheet features observed by FTIR. Electrospray ionization mass spectrometry indicates that NH 2 -K(Boc)LVFF-CONH 2 forms a significant population of oligomeric species above the cac. Cryo-TEM, used together with SAXS to determine fibril dimensions, shows that the length and degree of twisting of peptide fibrils seem to be influenced by the net peptide charge. Grazing incidence X-ray scattering from thin peptide films shows features of β-sheet ordering for both peptides, along with evidence for lamellar ordering of NH 2 -KLVFF-CONH 2. This work provides a comprehensive picture of the aggregation properties of these two KLVFF derivatives and shows their utility, in unaggregated form, in restoring the viability of neuroblastoma cells against Aβ-induced toxicity.Fil: Castelletto, V.. University of Reading; Reino UnidoFil: Ryumin, P.. University of Reading; Reino UnidoFil: Cramer, R.. University of Reading; Reino UnidoFil: Hamley, I.W.. University of Reading; Reino UnidoFil: Taylor, M.. University of Lancaster; Reino UnidoFil: Allsop, D.. University of Lancaster; Reino UnidoFil: Reza, M.. Aalto University; FinlandiaFil: Ruokolainen, J.. Aalto University; FinlandiaFil: Arnold, T.. Diamond Light Source Ltd.,Harwell Science and Innovation Campus; Reino UnidoFil: Hermida Merino, D.. European Synchrotron Radiation Facility; FranciaFil: Garcia, Corina Ileana. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; ArgentinaFil: Leal, Maria Celeste. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; ArgentinaFil: Castaño, Eduardo Miguel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; ArgentinaNature Publishing Group2017-03info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/92942Castelletto, V.; Ryumin, P.; Cramer, R.; Hamley, I.W.; Taylor, M.; et al.; Self-assembly and anti-amyloid cytotoxicity activity of amyloid beta peptide derivatives; Nature Publishing Group; Scientific Reports; 7; 3-20172045-2322CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://www.nature.com/articles/srep43637info:eu-repo/semantics/altIdentifier/doi/10.1038/srep43637info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:59:27Zoai:ri.conicet.gov.ar:11336/92942instacron: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 09:59:27.291CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Self-assembly and anti-amyloid cytotoxicity activity of amyloid beta peptide derivatives
title Self-assembly and anti-amyloid cytotoxicity activity of amyloid beta peptide derivatives
spellingShingle Self-assembly and anti-amyloid cytotoxicity activity of amyloid beta peptide derivatives
Castelletto, V.
Alzheimer Diseade
Amyloid Beta
Neurodegeneration
Amyloid Beta
title_short Self-assembly and anti-amyloid cytotoxicity activity of amyloid beta peptide derivatives
title_full Self-assembly and anti-amyloid cytotoxicity activity of amyloid beta peptide derivatives
title_fullStr Self-assembly and anti-amyloid cytotoxicity activity of amyloid beta peptide derivatives
title_full_unstemmed Self-assembly and anti-amyloid cytotoxicity activity of amyloid beta peptide derivatives
title_sort Self-assembly and anti-amyloid cytotoxicity activity of amyloid beta peptide derivatives
dc.creator.none.fl_str_mv Castelletto, V.
Ryumin, P.
Cramer, R.
Hamley, I.W.
Taylor, M.
Allsop, D.
Reza, M.
Ruokolainen, J.
Arnold, T.
Hermida Merino, D.
Garcia, Corina Ileana
Leal, Maria Celeste
Castaño, Eduardo Miguel
author Castelletto, V.
author_facet Castelletto, V.
Ryumin, P.
Cramer, R.
Hamley, I.W.
Taylor, M.
Allsop, D.
Reza, M.
Ruokolainen, J.
Arnold, T.
Hermida Merino, D.
Garcia, Corina Ileana
Leal, Maria Celeste
Castaño, Eduardo Miguel
author_role author
author2 Ryumin, P.
Cramer, R.
Hamley, I.W.
Taylor, M.
Allsop, D.
Reza, M.
Ruokolainen, J.
Arnold, T.
Hermida Merino, D.
Garcia, Corina Ileana
Leal, Maria Celeste
Castaño, Eduardo Miguel
author2_role author
author
author
author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Alzheimer Diseade
Amyloid Beta
Neurodegeneration
Amyloid Beta
topic Alzheimer Diseade
Amyloid Beta
Neurodegeneration
Amyloid Beta
purl_subject.fl_str_mv https://purl.org/becyt/ford/3.1
https://purl.org/becyt/ford/3
dc.description.none.fl_txt_mv The self-assembly of two derivatives of KLVFF, a fragment Aβ(16-20) of the amyloid beta (Aβ) peptide, is investigated and recovery of viability of neuroblastoma cells exposed to Aβ (1-42) is observed at sub-stoichiometric peptide concentrations. Fluorescence assays show that NH 2 -KLVFF-CONH 2 undergoes hydrophobic collapse and amyloid formation at the same critical aggregation concentration (cac). In contrast, NH 2 -K(Boc)LVFF-CONH 2 undergoes hydrophobic collapse at a low concentration, followed by amyloid formation at a higher cac. These findings are supported by the β-sheet features observed by FTIR. Electrospray ionization mass spectrometry indicates that NH 2 -K(Boc)LVFF-CONH 2 forms a significant population of oligomeric species above the cac. Cryo-TEM, used together with SAXS to determine fibril dimensions, shows that the length and degree of twisting of peptide fibrils seem to be influenced by the net peptide charge. Grazing incidence X-ray scattering from thin peptide films shows features of β-sheet ordering for both peptides, along with evidence for lamellar ordering of NH 2 -KLVFF-CONH 2. This work provides a comprehensive picture of the aggregation properties of these two KLVFF derivatives and shows their utility, in unaggregated form, in restoring the viability of neuroblastoma cells against Aβ-induced toxicity.
Fil: Castelletto, V.. University of Reading; Reino Unido
Fil: Ryumin, P.. University of Reading; Reino Unido
Fil: Cramer, R.. University of Reading; Reino Unido
Fil: Hamley, I.W.. University of Reading; Reino Unido
Fil: Taylor, M.. University of Lancaster; Reino Unido
Fil: Allsop, D.. University of Lancaster; Reino Unido
Fil: Reza, M.. Aalto University; Finlandia
Fil: Ruokolainen, J.. Aalto University; Finlandia
Fil: Arnold, T.. Diamond Light Source Ltd.,Harwell Science and Innovation Campus; Reino Unido
Fil: Hermida Merino, D.. European Synchrotron Radiation Facility; Francia
Fil: Garcia, Corina Ileana. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
Fil: Leal, Maria Celeste. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
Fil: Castaño, Eduardo Miguel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
description The self-assembly of two derivatives of KLVFF, a fragment Aβ(16-20) of the amyloid beta (Aβ) peptide, is investigated and recovery of viability of neuroblastoma cells exposed to Aβ (1-42) is observed at sub-stoichiometric peptide concentrations. Fluorescence assays show that NH 2 -KLVFF-CONH 2 undergoes hydrophobic collapse and amyloid formation at the same critical aggregation concentration (cac). In contrast, NH 2 -K(Boc)LVFF-CONH 2 undergoes hydrophobic collapse at a low concentration, followed by amyloid formation at a higher cac. These findings are supported by the β-sheet features observed by FTIR. Electrospray ionization mass spectrometry indicates that NH 2 -K(Boc)LVFF-CONH 2 forms a significant population of oligomeric species above the cac. Cryo-TEM, used together with SAXS to determine fibril dimensions, shows that the length and degree of twisting of peptide fibrils seem to be influenced by the net peptide charge. Grazing incidence X-ray scattering from thin peptide films shows features of β-sheet ordering for both peptides, along with evidence for lamellar ordering of NH 2 -KLVFF-CONH 2. This work provides a comprehensive picture of the aggregation properties of these two KLVFF derivatives and shows their utility, in unaggregated form, in restoring the viability of neuroblastoma cells against Aβ-induced toxicity.
publishDate 2017
dc.date.none.fl_str_mv 2017-03
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/11336/92942
Castelletto, V.; Ryumin, P.; Cramer, R.; Hamley, I.W.; Taylor, M.; et al.; Self-assembly and anti-amyloid cytotoxicity activity of amyloid beta peptide derivatives; Nature Publishing Group; Scientific Reports; 7; 3-2017
2045-2322
CONICET Digital
CONICET
url http://hdl.handle.net/11336/92942
identifier_str_mv Castelletto, V.; Ryumin, P.; Cramer, R.; Hamley, I.W.; Taylor, M.; et al.; Self-assembly and anti-amyloid cytotoxicity activity of amyloid beta peptide derivatives; Nature Publishing Group; Scientific Reports; 7; 3-2017
2045-2322
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.nature.com/articles/srep43637
info:eu-repo/semantics/altIdentifier/doi/10.1038/srep43637
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
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Nature Publishing Group
publisher.none.fl_str_mv Nature Publishing Group
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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