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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/196461
Ver los metadatos del registro completo
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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 Técnicas2025-09-29T09:47:25Zoai: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:34982025-09-29 09:47:25.701CONICET 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 |
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1844613478132744192 |
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13.070432 |