Negative Dipole Potentials and Carboxylic Polar Head Groups Foster the Insertion of Cell-Penetrating Peptides into Lipid Monolayers

Autores
Via, Matías Alejandro; del Popolo, Mario Gabriel; Wilke, Natalia
Año de publicación
2018
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Cell-penetrating peptides (CPPs) are polycationic sequences of amino acids recognized as some of the most effective vehicles for delivering membrane-impermeable cargos into cells. CPPs can traverse cell membranes by direct translocation, and assessing the role of lipids on the membrane permeation process is important to convene a complete model of the CPP translocation. In this work, we focus on the biophysical basis of peptide-fatty acid interactions, analyzing how the acid-base and electrostatic properties of the lipids determine the CPP adsorption and incorporation into a Langmuir monolayer, focusing thus on the first two stages of the direct translocation mechanism. We sense the binding and insertion of the peptide into the lipid structure by measuring the changes in the surface pressure, the surface potential, and the reflectivity of the interface. We show that, beyond the presence of anionic moieties, negative dipole potentials and carboxylic polar head groups significantly promote the insertion of the peptide into the monolayer. On the basis of our results, we propose the appearance of stable CPP-lipid complexes whose kinetics of formation depends on the length of the lipids' hydrocarbon chains.
Fil: Via, Matías Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos. Universidad Nacional de Cuyo. Facultad de Ciencias Médicas. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos; Argentina
Fil: del Popolo, Mario Gabriel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza; Argentina. Universidad Nacional de Cuyo. Facultad de Ciencias Exactas y Naturales; Argentina
Fil: Wilke, Natalia. 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. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Departamento de Química Biológica; Argentina
Materia
POLYARGININES
LIPID BILAYER
FATTY ACIDS
NEGATIVE DIPOLE
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:11336/95820
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/95820
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Negative Dipole Potentials and Carboxylic Polar Head Groups Foster the Insertion of Cell-Penetrating Peptides into Lipid MonolayersVia, Matías Alejandrodel Popolo, Mario GabrielWilke, NataliaPOLYARGININESLIPID BILAYERFATTY ACIDSNEGATIVE DIPOLEhttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1Cell-penetrating peptides (CPPs) are polycationic sequences of amino acids recognized as some of the most effective vehicles for delivering membrane-impermeable cargos into cells. CPPs can traverse cell membranes by direct translocation, and assessing the role of lipids on the membrane permeation process is important to convene a complete model of the CPP translocation. In this work, we focus on the biophysical basis of peptide-fatty acid interactions, analyzing how the acid-base and electrostatic properties of the lipids determine the CPP adsorption and incorporation into a Langmuir monolayer, focusing thus on the first two stages of the direct translocation mechanism. We sense the binding and insertion of the peptide into the lipid structure by measuring the changes in the surface pressure, the surface potential, and the reflectivity of the interface. We show that, beyond the presence of anionic moieties, negative dipole potentials and carboxylic polar head groups significantly promote the insertion of the peptide into the monolayer. On the basis of our results, we propose the appearance of stable CPP-lipid complexes whose kinetics of formation depends on the length of the lipids' hydrocarbon chains.Fil: Via, Matías Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos. Universidad Nacional de Cuyo. Facultad de Ciencias Médicas. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos; ArgentinaFil: del Popolo, Mario Gabriel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza; Argentina. Universidad Nacional de Cuyo. Facultad de Ciencias Exactas y Naturales; ArgentinaFil: Wilke, Natalia. 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. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Departamento de Química Biológica; ArgentinaAmerican Chemical Society2018-03info: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/11336/95820Via, Matías Alejandro; del Popolo, Mario Gabriel; Wilke, Natalia; Negative Dipole Potentials and Carboxylic Polar Head Groups Foster the Insertion of Cell-Penetrating Peptides into Lipid Monolayers; American Chemical Society; Langmuir; 34; 9; 3-2018; 3102-31110743-7463CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://pubs.acs.org/doi/10.1021/acs.langmuir.7b04038info:eu-repo/semantics/altIdentifier/doi/10.1021/acs.langmuir.7b04038info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:44:53Zoai:ri.conicet.gov.ar:11336/95820instacron: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 09:44:53.465CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Negative Dipole Potentials and Carboxylic Polar Head Groups Foster the Insertion of Cell-Penetrating Peptides into Lipid Monolayers
title Negative Dipole Potentials and Carboxylic Polar Head Groups Foster the Insertion of Cell-Penetrating Peptides into Lipid Monolayers
spellingShingle Negative Dipole Potentials and Carboxylic Polar Head Groups Foster the Insertion of Cell-Penetrating Peptides into Lipid Monolayers
Via, Matías Alejandro
POLYARGININES
LIPID BILAYER
FATTY ACIDS
NEGATIVE DIPOLE
title_short Negative Dipole Potentials and Carboxylic Polar Head Groups Foster the Insertion of Cell-Penetrating Peptides into Lipid Monolayers
title_full Negative Dipole Potentials and Carboxylic Polar Head Groups Foster the Insertion of Cell-Penetrating Peptides into Lipid Monolayers
title_fullStr Negative Dipole Potentials and Carboxylic Polar Head Groups Foster the Insertion of Cell-Penetrating Peptides into Lipid Monolayers
title_full_unstemmed Negative Dipole Potentials and Carboxylic Polar Head Groups Foster the Insertion of Cell-Penetrating Peptides into Lipid Monolayers
title_sort Negative Dipole Potentials and Carboxylic Polar Head Groups Foster the Insertion of Cell-Penetrating Peptides into Lipid Monolayers
dc.creator.none.fl_str_mv Via, Matías Alejandro
del Popolo, Mario Gabriel
Wilke, Natalia
author Via, Matías Alejandro
author_facet Via, Matías Alejandro
del Popolo, Mario Gabriel
Wilke, Natalia
author_role author
author2 del Popolo, Mario Gabriel
Wilke, Natalia
author2_role author
author
dc.subject.none.fl_str_mv POLYARGININES
LIPID BILAYER
FATTY ACIDS
NEGATIVE DIPOLE
topic POLYARGININES
LIPID BILAYER
FATTY ACIDS
NEGATIVE DIPOLE
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Cell-penetrating peptides (CPPs) are polycationic sequences of amino acids recognized as some of the most effective vehicles for delivering membrane-impermeable cargos into cells. CPPs can traverse cell membranes by direct translocation, and assessing the role of lipids on the membrane permeation process is important to convene a complete model of the CPP translocation. In this work, we focus on the biophysical basis of peptide-fatty acid interactions, analyzing how the acid-base and electrostatic properties of the lipids determine the CPP adsorption and incorporation into a Langmuir monolayer, focusing thus on the first two stages of the direct translocation mechanism. We sense the binding and insertion of the peptide into the lipid structure by measuring the changes in the surface pressure, the surface potential, and the reflectivity of the interface. We show that, beyond the presence of anionic moieties, negative dipole potentials and carboxylic polar head groups significantly promote the insertion of the peptide into the monolayer. On the basis of our results, we propose the appearance of stable CPP-lipid complexes whose kinetics of formation depends on the length of the lipids' hydrocarbon chains.
Fil: Via, Matías Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos. Universidad Nacional de Cuyo. Facultad de Ciencias Médicas. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos; Argentina
Fil: del Popolo, Mario Gabriel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza; Argentina. Universidad Nacional de Cuyo. Facultad de Ciencias Exactas y Naturales; Argentina
Fil: Wilke, Natalia. 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. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Departamento de Química Biológica; Argentina
description Cell-penetrating peptides (CPPs) are polycationic sequences of amino acids recognized as some of the most effective vehicles for delivering membrane-impermeable cargos into cells. CPPs can traverse cell membranes by direct translocation, and assessing the role of lipids on the membrane permeation process is important to convene a complete model of the CPP translocation. In this work, we focus on the biophysical basis of peptide-fatty acid interactions, analyzing how the acid-base and electrostatic properties of the lipids determine the CPP adsorption and incorporation into a Langmuir monolayer, focusing thus on the first two stages of the direct translocation mechanism. We sense the binding and insertion of the peptide into the lipid structure by measuring the changes in the surface pressure, the surface potential, and the reflectivity of the interface. We show that, beyond the presence of anionic moieties, negative dipole potentials and carboxylic polar head groups significantly promote the insertion of the peptide into the monolayer. On the basis of our results, we propose the appearance of stable CPP-lipid complexes whose kinetics of formation depends on the length of the lipids' hydrocarbon chains.
publishDate 2018
dc.date.none.fl_str_mv 2018-03
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/11336/95820
Via, Matías Alejandro; del Popolo, Mario Gabriel; Wilke, Natalia; Negative Dipole Potentials and Carboxylic Polar Head Groups Foster the Insertion of Cell-Penetrating Peptides into Lipid Monolayers; American Chemical Society; Langmuir; 34; 9; 3-2018; 3102-3111
0743-7463
CONICET Digital
CONICET
url http://hdl.handle.net/11336/95820
identifier_str_mv Via, Matías Alejandro; del Popolo, Mario Gabriel; Wilke, Natalia; Negative Dipole Potentials and Carboxylic Polar Head Groups Foster the Insertion of Cell-Penetrating Peptides into Lipid Monolayers; American Chemical Society; Langmuir; 34; 9; 3-2018; 3102-3111
0743-7463
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://pubs.acs.org/doi/10.1021/acs.langmuir.7b04038
info:eu-repo/semantics/altIdentifier/doi/10.1021/acs.langmuir.7b04038
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 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
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score 13.070432

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