Antiviral Lipopeptide-Cell Membrane Interaction Is Influenced by PEG Linker Length

Autores
Augusto, Marcelo T.; Hollmann, Axel; Porotto, Matteo; Moscona, Anne; Santos, Nuno C.
Año de publicación
2017
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
A set of lipopeptides was recently reported for their broad-spectrum antiviral activity against viruses belonging to the Paramyxoviridae family, including human parainfluenza virus type 3 and Nipah virus. Among them, the peptide with a 24-unit PEG linker connecting it to a cholesterol moiety (VG-PEG24-Chol) was found to be the best membrane fusion inhibitory peptide. Here, we evaluated the interaction of the same set of peptides with biomembrane model systems and isolated human peripheral blood mononuclear cells (PBMC). VG-PEG24-Chol showed the highest insertion rate and it was among the peptides that induced a larger change on the surface pressure of cholesterol rich membranes. This peptide also displayed a high affinity towards PBMC membranes. These data provide new information about the dynamics of peptide-membrane interactions of a specific group of antiviral peptides, known for their potential as multipotent paramyxovirus antivirals.
Fil: Augusto, Marcelo T.. Universidade de Lisboa. Instituto de Medicina Molecular; Portugal
Fil: Hollmann, Axel. Universidade de Lisboa. Instituto de Medicina Molecular; Portugal. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro de Investigaciones y Transferencia de Santiago del Estero. Universidad Nacional de Santiago del Estero. Centro de Investigaciones y Transferencia de Santiago del Estero; Argentina. Universidad Nacional de Quilmes; Argentina
Fil: Porotto, Matteo. Columbia University Medical Center; Estados Unidos
Fil: Moscona, Anne. Columbia University Medical Center; Estados Unidos
Fil: Santos, Nuno C.. Universidade de Lisboa. Instituto de Medicina Molecular; Portugal
Materia
PARAMYXOVIRUSES
PEPTIDES
ANTIVIRAL
CHOLESTEROL
MEMBRANES
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/40899
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/40899
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Antiviral Lipopeptide-Cell Membrane Interaction Is Influenced by PEG Linker LengthAugusto, Marcelo T.Hollmann, AxelPorotto, MatteoMoscona, AnneSantos, Nuno C.PARAMYXOVIRUSESPEPTIDESANTIVIRALCHOLESTEROLMEMBRANEShttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1A set of lipopeptides was recently reported for their broad-spectrum antiviral activity against viruses belonging to the Paramyxoviridae family, including human parainfluenza virus type 3 and Nipah virus. Among them, the peptide with a 24-unit PEG linker connecting it to a cholesterol moiety (VG-PEG24-Chol) was found to be the best membrane fusion inhibitory peptide. Here, we evaluated the interaction of the same set of peptides with biomembrane model systems and isolated human peripheral blood mononuclear cells (PBMC). VG-PEG24-Chol showed the highest insertion rate and it was among the peptides that induced a larger change on the surface pressure of cholesterol rich membranes. This peptide also displayed a high affinity towards PBMC membranes. These data provide new information about the dynamics of peptide-membrane interactions of a specific group of antiviral peptides, known for their potential as multipotent paramyxovirus antivirals.Fil: Augusto, Marcelo T.. Universidade de Lisboa. Instituto de Medicina Molecular; PortugalFil: Hollmann, Axel. Universidade de Lisboa. Instituto de Medicina Molecular; Portugal. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro de Investigaciones y Transferencia de Santiago del Estero. Universidad Nacional de Santiago del Estero. Centro de Investigaciones y Transferencia de Santiago del Estero; Argentina. Universidad Nacional de Quilmes; ArgentinaFil: Porotto, Matteo. Columbia University Medical Center; Estados UnidosFil: Moscona, Anne. Columbia University Medical Center; Estados UnidosFil: Santos, Nuno C.. Universidade de Lisboa. Instituto de Medicina Molecular; PortugalMolecular Diversity Preservation International2017-07info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/40899Augusto, Marcelo T.; Hollmann, Axel; Porotto, Matteo; Moscona, Anne; Santos, Nuno C.; Antiviral Lipopeptide-Cell Membrane Interaction Is Influenced by PEG Linker Length; Molecular Diversity Preservation International; Molecules; 22; 7; 7-20171420-3049CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://www.mdpi.com/1420-3049/22/7/1190info:eu-repo/semantics/altIdentifier/doi/10.3390/molecules22071190info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:40:55Zoai:ri.conicet.gov.ar:11336/40899instacron: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:34982025-09-29 09:40:55.347CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Antiviral Lipopeptide-Cell Membrane Interaction Is Influenced by PEG Linker Length
title Antiviral Lipopeptide-Cell Membrane Interaction Is Influenced by PEG Linker Length
spellingShingle Antiviral Lipopeptide-Cell Membrane Interaction Is Influenced by PEG Linker Length
Augusto, Marcelo T.
PARAMYXOVIRUSES
PEPTIDES
ANTIVIRAL
CHOLESTEROL
MEMBRANES
title_short Antiviral Lipopeptide-Cell Membrane Interaction Is Influenced by PEG Linker Length
title_full Antiviral Lipopeptide-Cell Membrane Interaction Is Influenced by PEG Linker Length
title_fullStr Antiviral Lipopeptide-Cell Membrane Interaction Is Influenced by PEG Linker Length
title_full_unstemmed Antiviral Lipopeptide-Cell Membrane Interaction Is Influenced by PEG Linker Length
title_sort Antiviral Lipopeptide-Cell Membrane Interaction Is Influenced by PEG Linker Length
dc.creator.none.fl_str_mv Augusto, Marcelo T.
Hollmann, Axel
Porotto, Matteo
Moscona, Anne
Santos, Nuno C.
author Augusto, Marcelo T.
author_facet Augusto, Marcelo T.
Hollmann, Axel
Porotto, Matteo
Moscona, Anne
Santos, Nuno C.
author_role author
author2 Hollmann, Axel
Porotto, Matteo
Moscona, Anne
Santos, Nuno C.
author2_role author
author
author
author
dc.subject.none.fl_str_mv PARAMYXOVIRUSES
PEPTIDES
ANTIVIRAL
CHOLESTEROL
MEMBRANES
topic PARAMYXOVIRUSES
PEPTIDES
ANTIVIRAL
CHOLESTEROL
MEMBRANES
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv A set of lipopeptides was recently reported for their broad-spectrum antiviral activity against viruses belonging to the Paramyxoviridae family, including human parainfluenza virus type 3 and Nipah virus. Among them, the peptide with a 24-unit PEG linker connecting it to a cholesterol moiety (VG-PEG24-Chol) was found to be the best membrane fusion inhibitory peptide. Here, we evaluated the interaction of the same set of peptides with biomembrane model systems and isolated human peripheral blood mononuclear cells (PBMC). VG-PEG24-Chol showed the highest insertion rate and it was among the peptides that induced a larger change on the surface pressure of cholesterol rich membranes. This peptide also displayed a high affinity towards PBMC membranes. These data provide new information about the dynamics of peptide-membrane interactions of a specific group of antiviral peptides, known for their potential as multipotent paramyxovirus antivirals.
Fil: Augusto, Marcelo T.. Universidade de Lisboa. Instituto de Medicina Molecular; Portugal
Fil: Hollmann, Axel. Universidade de Lisboa. Instituto de Medicina Molecular; Portugal. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro de Investigaciones y Transferencia de Santiago del Estero. Universidad Nacional de Santiago del Estero. Centro de Investigaciones y Transferencia de Santiago del Estero; Argentina. Universidad Nacional de Quilmes; Argentina
Fil: Porotto, Matteo. Columbia University Medical Center; Estados Unidos
Fil: Moscona, Anne. Columbia University Medical Center; Estados Unidos
Fil: Santos, Nuno C.. Universidade de Lisboa. Instituto de Medicina Molecular; Portugal
description A set of lipopeptides was recently reported for their broad-spectrum antiviral activity against viruses belonging to the Paramyxoviridae family, including human parainfluenza virus type 3 and Nipah virus. Among them, the peptide with a 24-unit PEG linker connecting it to a cholesterol moiety (VG-PEG24-Chol) was found to be the best membrane fusion inhibitory peptide. Here, we evaluated the interaction of the same set of peptides with biomembrane model systems and isolated human peripheral blood mononuclear cells (PBMC). VG-PEG24-Chol showed the highest insertion rate and it was among the peptides that induced a larger change on the surface pressure of cholesterol rich membranes. This peptide also displayed a high affinity towards PBMC membranes. These data provide new information about the dynamics of peptide-membrane interactions of a specific group of antiviral peptides, known for their potential as multipotent paramyxovirus antivirals.
publishDate 2017
dc.date.none.fl_str_mv 2017-07
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/11336/40899
Augusto, Marcelo T.; Hollmann, Axel; Porotto, Matteo; Moscona, Anne; Santos, Nuno C.; Antiviral Lipopeptide-Cell Membrane Interaction Is Influenced by PEG Linker Length; Molecular Diversity Preservation International; Molecules; 22; 7; 7-2017
1420-3049
CONICET Digital
CONICET
url http://hdl.handle.net/11336/40899
identifier_str_mv Augusto, Marcelo T.; Hollmann, Axel; Porotto, Matteo; Moscona, Anne; Santos, Nuno C.; Antiviral Lipopeptide-Cell Membrane Interaction Is Influenced by PEG Linker Length; Molecular Diversity Preservation International; Molecules; 22; 7; 7-2017
1420-3049
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.mdpi.com/1420-3049/22/7/1190
info:eu-repo/semantics/altIdentifier/doi/10.3390/molecules22071190
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Molecular Diversity Preservation International
publisher.none.fl_str_mv Molecular Diversity Preservation International
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 13.070432

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