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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/189768
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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 Técnicas2025-09-29T10:45:52Zoai: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:34982025-09-29 10:45:53.145CONICET 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_ |
1844614499295821824 |
score |
13.070432 |