Oligoarginine vectors for intracellular delivery: Role of arginine side-chain orientation in chain length-dependent destabilization of lipid membranes

Autores
Bouchet, Ana María; Lairion, F.; Ruysschaert, J. M.; Lensink, M. F.
Año de publicación
2012
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Arginine-rich peptides receive increased attention due to their capacity to cross different types of membranes and to transport cargo molecules inside cells. Even though peptide-induced destabilization has been investigated extensively, little is known about the peptide side-chain and backbone orientation with respect to the bilayer that may contribute to a molecular understanding of the peptide-induced membrane perturbations. The main objective of this work is to provide a detailed description of the orientation of arginine peptides in the lipid bilayer of PC and negatively charged PG liposomes using ATR-IR spectroscopy and molecular modeling, and to relate these orientational preferences to lipid bilayer destabilization. Molecular modeling showed that above the transition temperature arginine side-chains are preferentially solvent-directed at the PC/water interface whereas several arginine side-chains are pointing towards the PG hydrophobic core. IR dichroic spectra confirmed the orientation of the arginine side chains perpendicular to the lipid-water interface. IR spectra shows an randomly distributed backbone that seems essential to optimize interactions with the lipid membrane. The observed increase of permeation to a fluorescent dye is related to the peptide induced-formation of gauche bonds in the acyl chains. In the absence of hydrophobic residues, insertion of side-chains that favors phosphate/guanidium interaction is another mechanism of membrane permeabilization that has not been further analyzed so far.
Fil: Bouchet, Ana María. Université Libre de Bruxelles; Bélgica. Universidad de Buenos Aires; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Lairion, F.. Universidad de Buenos Aires; Argentina
Fil: Ruysschaert, J. M.. Université Libre de Bruxelles; Bélgica
Fil: Lensink, M. F.. Université Libre de Bruxelles; Bélgica
Materia
ATR-FTIR
BILAYER DESTABILIZATION
CELL-PENETRATING PEPTIDE
LIPIDS
MOLECULAR DYNAMICS
OLIGOARGININE
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:11336/189768
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/189768
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Oligoarginine vectors for intracellular delivery: Role of arginine side-chain orientation in chain length-dependent destabilization of lipid membranesBouchet, Ana MaríaLairion, F.Ruysschaert, J. M.Lensink, M. F.ATR-FTIRBILAYER DESTABILIZATIONCELL-PENETRATING PEPTIDELIPIDSMOLECULAR DYNAMICSOLIGOARGININEhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Arginine-rich peptides receive increased attention due to their capacity to cross different types of membranes and to transport cargo molecules inside cells. Even though peptide-induced destabilization has been investigated extensively, little is known about the peptide side-chain and backbone orientation with respect to the bilayer that may contribute to a molecular understanding of the peptide-induced membrane perturbations. The main objective of this work is to provide a detailed description of the orientation of arginine peptides in the lipid bilayer of PC and negatively charged PG liposomes using ATR-IR spectroscopy and molecular modeling, and to relate these orientational preferences to lipid bilayer destabilization. Molecular modeling showed that above the transition temperature arginine side-chains are preferentially solvent-directed at the PC/water interface whereas several arginine side-chains are pointing towards the PG hydrophobic core. IR dichroic spectra confirmed the orientation of the arginine side chains perpendicular to the lipid-water interface. IR spectra shows an randomly distributed backbone that seems essential to optimize interactions with the lipid membrane. The observed increase of permeation to a fluorescent dye is related to the peptide induced-formation of gauche bonds in the acyl chains. In the absence of hydrophobic residues, insertion of side-chains that favors phosphate/guanidium interaction is another mechanism of membrane permeabilization that has not been further analyzed so far.Fil: Bouchet, Ana María. Université Libre de Bruxelles; Bélgica. Universidad de Buenos Aires; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Lairion, F.. Universidad de Buenos Aires; ArgentinaFil: Ruysschaert, J. M.. Université Libre de Bruxelles; BélgicaFil: Lensink, M. F.. Université Libre de Bruxelles; BélgicaElsevier Ireland2012-04info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/189768Bouchet, Ana María; Lairion, F.; Ruysschaert, J. M.; Lensink, M. F.; Oligoarginine vectors for intracellular delivery: Role of arginine side-chain orientation in chain length-dependent destabilization of lipid membranes; Elsevier Ireland; Chemistry and Physics of Lipids; 165; 1; 4-2012; 89-960009-3084CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0009308411003550info:eu-repo/semantics/altIdentifier/doi/10.1016/j.chemphyslip.2011.11.008info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T12:19:12Zoai:ri.conicet.gov.ar:11336/189768instacron: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:34982025-10-22 12:19:12.968CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Oligoarginine vectors for intracellular delivery: Role of arginine side-chain orientation in chain length-dependent destabilization of lipid membranes
title Oligoarginine vectors for intracellular delivery: Role of arginine side-chain orientation in chain length-dependent destabilization of lipid membranes
spellingShingle Oligoarginine vectors for intracellular delivery: Role of arginine side-chain orientation in chain length-dependent destabilization of lipid membranes
Bouchet, Ana María
ATR-FTIR
BILAYER DESTABILIZATION
CELL-PENETRATING PEPTIDE
LIPIDS
MOLECULAR DYNAMICS
OLIGOARGININE
title_short Oligoarginine vectors for intracellular delivery: Role of arginine side-chain orientation in chain length-dependent destabilization of lipid membranes
title_full Oligoarginine vectors for intracellular delivery: Role of arginine side-chain orientation in chain length-dependent destabilization of lipid membranes
title_fullStr Oligoarginine vectors for intracellular delivery: Role of arginine side-chain orientation in chain length-dependent destabilization of lipid membranes
title_full_unstemmed Oligoarginine vectors for intracellular delivery: Role of arginine side-chain orientation in chain length-dependent destabilization of lipid membranes
title_sort Oligoarginine vectors for intracellular delivery: Role of arginine side-chain orientation in chain length-dependent destabilization of lipid membranes
dc.creator.none.fl_str_mv Bouchet, Ana María
Lairion, F.
Ruysschaert, J. M.
Lensink, M. F.
author Bouchet, Ana María
author_facet Bouchet, Ana María
Lairion, F.
Ruysschaert, J. M.
Lensink, M. F.
author_role author
author2 Lairion, F.
Ruysschaert, J. M.
Lensink, M. F.
author2_role author
author
author
dc.subject.none.fl_str_mv ATR-FTIR
BILAYER DESTABILIZATION
CELL-PENETRATING PEPTIDE
LIPIDS
MOLECULAR DYNAMICS
OLIGOARGININE
topic ATR-FTIR
BILAYER DESTABILIZATION
CELL-PENETRATING PEPTIDE
LIPIDS
MOLECULAR DYNAMICS
OLIGOARGININE
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Arginine-rich peptides receive increased attention due to their capacity to cross different types of membranes and to transport cargo molecules inside cells. Even though peptide-induced destabilization has been investigated extensively, little is known about the peptide side-chain and backbone orientation with respect to the bilayer that may contribute to a molecular understanding of the peptide-induced membrane perturbations. The main objective of this work is to provide a detailed description of the orientation of arginine peptides in the lipid bilayer of PC and negatively charged PG liposomes using ATR-IR spectroscopy and molecular modeling, and to relate these orientational preferences to lipid bilayer destabilization. Molecular modeling showed that above the transition temperature arginine side-chains are preferentially solvent-directed at the PC/water interface whereas several arginine side-chains are pointing towards the PG hydrophobic core. IR dichroic spectra confirmed the orientation of the arginine side chains perpendicular to the lipid-water interface. IR spectra shows an randomly distributed backbone that seems essential to optimize interactions with the lipid membrane. The observed increase of permeation to a fluorescent dye is related to the peptide induced-formation of gauche bonds in the acyl chains. In the absence of hydrophobic residues, insertion of side-chains that favors phosphate/guanidium interaction is another mechanism of membrane permeabilization that has not been further analyzed so far.
Fil: Bouchet, Ana María. Université Libre de Bruxelles; Bélgica. Universidad de Buenos Aires; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Lairion, F.. Universidad de Buenos Aires; Argentina
Fil: Ruysschaert, J. M.. Université Libre de Bruxelles; Bélgica
Fil: Lensink, M. F.. Université Libre de Bruxelles; Bélgica
description Arginine-rich peptides receive increased attention due to their capacity to cross different types of membranes and to transport cargo molecules inside cells. Even though peptide-induced destabilization has been investigated extensively, little is known about the peptide side-chain and backbone orientation with respect to the bilayer that may contribute to a molecular understanding of the peptide-induced membrane perturbations. The main objective of this work is to provide a detailed description of the orientation of arginine peptides in the lipid bilayer of PC and negatively charged PG liposomes using ATR-IR spectroscopy and molecular modeling, and to relate these orientational preferences to lipid bilayer destabilization. Molecular modeling showed that above the transition temperature arginine side-chains are preferentially solvent-directed at the PC/water interface whereas several arginine side-chains are pointing towards the PG hydrophobic core. IR dichroic spectra confirmed the orientation of the arginine side chains perpendicular to the lipid-water interface. IR spectra shows an randomly distributed backbone that seems essential to optimize interactions with the lipid membrane. The observed increase of permeation to a fluorescent dye is related to the peptide induced-formation of gauche bonds in the acyl chains. In the absence of hydrophobic residues, insertion of side-chains that favors phosphate/guanidium interaction is another mechanism of membrane permeabilization that has not been further analyzed so far.
publishDate 2012
dc.date.none.fl_str_mv 2012-04
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/11336/189768
Bouchet, Ana María; Lairion, F.; Ruysschaert, J. M.; Lensink, M. F.; Oligoarginine vectors for intracellular delivery: Role of arginine side-chain orientation in chain length-dependent destabilization of lipid membranes; Elsevier Ireland; Chemistry and Physics of Lipids; 165; 1; 4-2012; 89-96
0009-3084
CONICET Digital
CONICET
url http://hdl.handle.net/11336/189768
identifier_str_mv Bouchet, Ana María; Lairion, F.; Ruysschaert, J. M.; Lensink, M. F.; Oligoarginine vectors for intracellular delivery: Role of arginine side-chain orientation in chain length-dependent destabilization of lipid membranes; Elsevier Ireland; Chemistry and Physics of Lipids; 165; 1; 4-2012; 89-96
0009-3084
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0009308411003550
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.chemphyslip.2011.11.008
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 Elsevier Ireland
publisher.none.fl_str_mv Elsevier Ireland
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
_version_ 1846782628794990592
score 12.982451

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