Amyloid formation by short peptides in the presence of dipalmitoylphosphatidylcholine membranes
Autor(a) principal: | |
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Data de Publicação: | 2020 |
Outros Autores: | , , , |
Tipo de documento: | Artigo |
Idioma: | por |
Título da fonte: | Repositório Institucional da UNIFESP |
Texto Completo: | https://repositorio.unifesp.br/11600/67484 |
Resumo: | The aggregation of two short peptides [RF] and [RF]4 (where R = arginine and F = phenylalanine) with dipalmitoylphosphatidylcholine (DPPC) model membranes was investigated at the air-water interface using the Langmuir technique and vesicles in aqueous solutions. The molar ratio of the peptide and lipid components was varied to provide insights into the peptide-membrane interactions, which might be related to their cytotoxicity.1 Both peptides exhibited affinity to the DPPC membrane interface and rapidly adopted β-sheet rich structures upon adsorption onto the surface of the zwitterionic membrane. Results from adsorption isotherm and small angle X-ray scattering (SAXS) experiments showed changes in the structural and thermodynamics parameters of the membrane with the increase in peptide concentration. Using atomic force microscopy (AFM), we showed the appearance of pores through the bilayer membranes and peptide aggregation at different interfaces, suggesting that the hydrophobic residues might have an effect on both pore size and layer structure, facilitating the membrane disruption and leading to different cytotoxicity effects. |
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Repositório Institucional da UNIFESP |
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3465 |
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da Silva, Emerson Rodrigo [UNIFESP]Gerbelli, Barbara BiancaAlves, Wendel AndradeOliveira, Cristiano Luis PintoHamley, Ianhttp://lattes.cnpq.br/78005892064573262023-05-11T13:06:04Z2023-05-11T13:06:04Z2020-11-19https://repositorio.unifesp.br/11600/67484The aggregation of two short peptides [RF] and [RF]4 (where R = arginine and F = phenylalanine) with dipalmitoylphosphatidylcholine (DPPC) model membranes was investigated at the air-water interface using the Langmuir technique and vesicles in aqueous solutions. The molar ratio of the peptide and lipid components was varied to provide insights into the peptide-membrane interactions, which might be related to their cytotoxicity.1 Both peptides exhibited affinity to the DPPC membrane interface and rapidly adopted β-sheet rich structures upon adsorption onto the surface of the zwitterionic membrane. Results from adsorption isotherm and small angle X-ray scattering (SAXS) experiments showed changes in the structural and thermodynamics parameters of the membrane with the increase in peptide concentration. Using atomic force microscopy (AFM), we showed the appearance of pores through the bilayer membranes and peptide aggregation at different interfaces, suggesting that the hydrophobic residues might have an effect on both pore size and layer structure, facilitating the membrane disruption and leading to different cytotoxicity effects.Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)19/20907-714793–14801porAmerican Chemical SocietyLangmuirLangmuir-blodgett filmsLipid monolayersAmyloidAtomic force microscopySmall-angle X-ray ScatteringAmyloid formation by short peptides in the presence of dipalmitoylphosphatidylcholine membranesinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article3648info:eu-repo/semantics/openAccessreponame:Repositório Institucional da UNIFESPinstname:Universidade Federal de São Paulo (UNIFESP)instacron:UNIFESPEscola Paulista de Medicina (EPM)Ciências Biológicas (Biologia Molecular)Biofísica 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InstitucionalPUBhttp://www.repositorio.unifesp.br/oai/requestopendoar:34652023-10-05T04:01:31Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP)false |
dc.title.en.fl_str_mv |
Amyloid formation by short peptides in the presence of dipalmitoylphosphatidylcholine membranes |
title |
Amyloid formation by short peptides in the presence of dipalmitoylphosphatidylcholine membranes |
spellingShingle |
Amyloid formation by short peptides in the presence of dipalmitoylphosphatidylcholine membranes da Silva, Emerson Rodrigo [UNIFESP] Langmuir-blodgett films Lipid monolayers Amyloid Atomic force microscopy Small-angle X-ray Scattering |
title_short |
Amyloid formation by short peptides in the presence of dipalmitoylphosphatidylcholine membranes |
title_full |
Amyloid formation by short peptides in the presence of dipalmitoylphosphatidylcholine membranes |
title_fullStr |
Amyloid formation by short peptides in the presence of dipalmitoylphosphatidylcholine membranes |
title_full_unstemmed |
Amyloid formation by short peptides in the presence of dipalmitoylphosphatidylcholine membranes |
title_sort |
Amyloid formation by short peptides in the presence of dipalmitoylphosphatidylcholine membranes |
author |
da Silva, Emerson Rodrigo [UNIFESP] |
author_facet |
da Silva, Emerson Rodrigo [UNIFESP] Gerbelli, Barbara Bianca Alves, Wendel Andrade Oliveira, Cristiano Luis Pinto Hamley, Ian |
author_role |
author |
author2 |
Gerbelli, Barbara Bianca Alves, Wendel Andrade Oliveira, Cristiano Luis Pinto Hamley, Ian |
author2_role |
author author author author |
dc.contributor.authorLattes.pt_BR.fl_str_mv |
http://lattes.cnpq.br/7800589206457326 |
dc.contributor.author.fl_str_mv |
da Silva, Emerson Rodrigo [UNIFESP] Gerbelli, Barbara Bianca Alves, Wendel Andrade Oliveira, Cristiano Luis Pinto Hamley, Ian |
dc.subject.e.fl_str_mv |
Langmuir-blodgett films |
topic |
Langmuir-blodgett films Lipid monolayers Amyloid Atomic force microscopy Small-angle X-ray Scattering |
dc.subject.eng.fl_str_mv |
Lipid monolayers Amyloid Atomic force microscopy Small-angle X-ray Scattering |
description |
The aggregation of two short peptides [RF] and [RF]4 (where R = arginine and F = phenylalanine) with dipalmitoylphosphatidylcholine (DPPC) model membranes was investigated at the air-water interface using the Langmuir technique and vesicles in aqueous solutions. The molar ratio of the peptide and lipid components was varied to provide insights into the peptide-membrane interactions, which might be related to their cytotoxicity.1 Both peptides exhibited affinity to the DPPC membrane interface and rapidly adopted β-sheet rich structures upon adsorption onto the surface of the zwitterionic membrane. Results from adsorption isotherm and small angle X-ray scattering (SAXS) experiments showed changes in the structural and thermodynamics parameters of the membrane with the increase in peptide concentration. Using atomic force microscopy (AFM), we showed the appearance of pores through the bilayer membranes and peptide aggregation at different interfaces, suggesting that the hydrophobic residues might have an effect on both pore size and layer structure, facilitating the membrane disruption and leading to different cytotoxicity effects. |
publishDate |
2020 |
dc.date.issued.fl_str_mv |
2020-11-19 |
dc.date.accessioned.fl_str_mv |
2023-05-11T13:06:04Z |
dc.date.available.fl_str_mv |
2023-05-11T13:06:04Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
https://repositorio.unifesp.br/11600/67484 |
url |
https://repositorio.unifesp.br/11600/67484 |
dc.language.iso.fl_str_mv |
por |
language |
por |
dc.relation.ispartof.pt_BR.fl_str_mv |
Langmuir |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
14793–14801 |
dc.publisher.none.fl_str_mv |
American Chemical Society |
publisher.none.fl_str_mv |
American Chemical Society |
dc.source.none.fl_str_mv |
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