Methylation of ethanolamine groups in phosphoethanolamines is relevant for L-arginine insertion in lipid membranes

Autores
Bouchet, Ana María; Lairion, Fabiana Norma; Disalvo, Edgardo Anibal
Año de publicación
2012
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The interaction of L-arginine with membranes composed by phospholipids with different degrees of methylation of the ethanolamine group was studied by means of surface and dipole potentials and surface pressure variations. The subsequent methylation of the amine head group appears to hinder the synergic response of the adsorption observed in phosphatidylethanolamine membranes. The kinetics of the binding process denotes that the methyl groups are relevant in regulating the specific interaction of the amino acid with the interface by hydrogen bonds. This response can be put in correlation with the function of signal transduction assigned previously to methyl lipids [F. Hirata and J. Axelrod, 1980] and appears to be relevant to understand the mechanism of insertion of arginine residues in peptides of biological interest.
Fil: Bouchet, Ana María. Universidad de Buenos Aires; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Lairion, Fabiana Norma. Universidad de Buenos Aires; Argentina
Fil: Disalvo, Edgardo Anibal. Universidad de Buenos Aires; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Materia
ARGININE
ISOTHERM ADSORPTION
PHOSPHATIDYLCHOLINE
PHOSPHATIDYLETHANOLAMINE
PHOSPHATIDYLETHANOLAMINE-METHYL DERIVATES
SURFACE PRESSURE
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:11336/196461
Acceder
id CONICETDig_28d3897313d4722c400b79ec06f7c506
oai_identifier_str oai:ri.conicet.gov.ar:11336/196461
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Methylation of ethanolamine groups in phosphoethanolamines is relevant for L-arginine insertion in lipid membranesBouchet, Ana MaríaLairion, Fabiana NormaDisalvo, Edgardo AnibalARGININEISOTHERM ADSORPTIONPHOSPHATIDYLCHOLINEPHOSPHATIDYLETHANOLAMINEPHOSPHATIDYLETHANOLAMINE-METHYL DERIVATESSURFACE PRESSUREhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The interaction of L-arginine with membranes composed by phospholipids with different degrees of methylation of the ethanolamine group was studied by means of surface and dipole potentials and surface pressure variations. The subsequent methylation of the amine head group appears to hinder the synergic response of the adsorption observed in phosphatidylethanolamine membranes. The kinetics of the binding process denotes that the methyl groups are relevant in regulating the specific interaction of the amino acid with the interface by hydrogen bonds. This response can be put in correlation with the function of signal transduction assigned previously to methyl lipids [F. Hirata and J. Axelrod, 1980] and appears to be relevant to understand the mechanism of insertion of arginine residues in peptides of biological interest.Fil: Bouchet, Ana María. Universidad de Buenos Aires; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Lairion, Fabiana Norma. Universidad de Buenos Aires; ArgentinaFil: Disalvo, Edgardo Anibal. Universidad de Buenos Aires; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaElsevier Science2012-06info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/196461Bouchet, Ana María; Lairion, Fabiana Norma; Disalvo, Edgardo Anibal; Methylation of ethanolamine groups in phosphoethanolamines is relevant for L-arginine insertion in lipid membranes; Elsevier Science; Biochimica et Biophysica Acta - Biomembranes; 1818; 5; 6-2012; 1395-14010005-2736CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0005273612000624info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bbamem.2012.02.011info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T11:16:18Zoai:ri.conicet.gov.ar:11336/196461instacron: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 11:16:18.646CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Methylation of ethanolamine groups in phosphoethanolamines is relevant for L-arginine insertion in lipid membranes
title Methylation of ethanolamine groups in phosphoethanolamines is relevant for L-arginine insertion in lipid membranes
spellingShingle Methylation of ethanolamine groups in phosphoethanolamines is relevant for L-arginine insertion in lipid membranes
Bouchet, Ana María
ARGININE
ISOTHERM ADSORPTION
PHOSPHATIDYLCHOLINE
PHOSPHATIDYLETHANOLAMINE
PHOSPHATIDYLETHANOLAMINE-METHYL DERIVATES
SURFACE PRESSURE
title_short Methylation of ethanolamine groups in phosphoethanolamines is relevant for L-arginine insertion in lipid membranes
title_full Methylation of ethanolamine groups in phosphoethanolamines is relevant for L-arginine insertion in lipid membranes
title_fullStr Methylation of ethanolamine groups in phosphoethanolamines is relevant for L-arginine insertion in lipid membranes
title_full_unstemmed Methylation of ethanolamine groups in phosphoethanolamines is relevant for L-arginine insertion in lipid membranes
title_sort Methylation of ethanolamine groups in phosphoethanolamines is relevant for L-arginine insertion in lipid membranes
dc.creator.none.fl_str_mv Bouchet, Ana María
Lairion, Fabiana Norma
Disalvo, Edgardo Anibal
author Bouchet, Ana María
author_facet Bouchet, Ana María
Lairion, Fabiana Norma
Disalvo, Edgardo Anibal
author_role author
author2 Lairion, Fabiana Norma
Disalvo, Edgardo Anibal
author2_role author
author
dc.subject.none.fl_str_mv ARGININE
ISOTHERM ADSORPTION
PHOSPHATIDYLCHOLINE
PHOSPHATIDYLETHANOLAMINE
PHOSPHATIDYLETHANOLAMINE-METHYL DERIVATES
SURFACE PRESSURE
topic ARGININE
ISOTHERM ADSORPTION
PHOSPHATIDYLCHOLINE
PHOSPHATIDYLETHANOLAMINE
PHOSPHATIDYLETHANOLAMINE-METHYL DERIVATES
SURFACE PRESSURE
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv The interaction of L-arginine with membranes composed by phospholipids with different degrees of methylation of the ethanolamine group was studied by means of surface and dipole potentials and surface pressure variations. The subsequent methylation of the amine head group appears to hinder the synergic response of the adsorption observed in phosphatidylethanolamine membranes. The kinetics of the binding process denotes that the methyl groups are relevant in regulating the specific interaction of the amino acid with the interface by hydrogen bonds. This response can be put in correlation with the function of signal transduction assigned previously to methyl lipids [F. Hirata and J. Axelrod, 1980] and appears to be relevant to understand the mechanism of insertion of arginine residues in peptides of biological interest.
Fil: Bouchet, Ana María. Universidad de Buenos Aires; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Lairion, Fabiana Norma. Universidad de Buenos Aires; Argentina
Fil: Disalvo, Edgardo Anibal. Universidad de Buenos Aires; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
description The interaction of L-arginine with membranes composed by phospholipids with different degrees of methylation of the ethanolamine group was studied by means of surface and dipole potentials and surface pressure variations. The subsequent methylation of the amine head group appears to hinder the synergic response of the adsorption observed in phosphatidylethanolamine membranes. The kinetics of the binding process denotes that the methyl groups are relevant in regulating the specific interaction of the amino acid with the interface by hydrogen bonds. This response can be put in correlation with the function of signal transduction assigned previously to methyl lipids [F. Hirata and J. Axelrod, 1980] and appears to be relevant to understand the mechanism of insertion of arginine residues in peptides of biological interest.
publishDate 2012
dc.date.none.fl_str_mv 2012-06
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/11336/196461
Bouchet, Ana María; Lairion, Fabiana Norma; Disalvo, Edgardo Anibal; Methylation of ethanolamine groups in phosphoethanolamines is relevant for L-arginine insertion in lipid membranes; Elsevier Science; Biochimica et Biophysica Acta - Biomembranes; 1818; 5; 6-2012; 1395-1401
0005-2736
CONICET Digital
CONICET
url http://hdl.handle.net/11336/196461
identifier_str_mv Bouchet, Ana María; Lairion, Fabiana Norma; Disalvo, Edgardo Anibal; Methylation of ethanolamine groups in phosphoethanolamines is relevant for L-arginine insertion in lipid membranes; Elsevier Science; Biochimica et Biophysica Acta - Biomembranes; 1818; 5; 6-2012; 1395-1401
0005-2736
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/S0005273612000624
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bbamem.2012.02.011
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
dc.publisher.none.fl_str_mv Elsevier Science
publisher.none.fl_str_mv Elsevier Science
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_ 1846781609708093440
score 13.234792

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