Molecular-level insight into the binding of arginine to a zwitterionic Langmuir monolayer

Autores
Klug, Joaquín; Masone, Diego Fernando; del Popolo, Mario Gabriel
Año de publicación
2017
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Solutions of the cationic amino-acid arginine (Arg+) in contact with a phospholipid monolayer are investigated by molecular dynamics simulations. The results show that Arg+ binds strongly to the lipid/water interface, with adsorption free-energies ranging from -43.8 to -22.2 kJ mol-1, depending on the amino-acids concentration. The large binding energies are attributed to hydrogen bonding between the charged moieties Arg+ and the phosphate and carbonyl groups of the phospholipids, that compensate for changes in the levels of hydration upon adsorption. We show that a concentrated layer of Arg+, tightly bound to the interface, has little effect on the compression isotherm and the lateral mechanical properties of the monolayer, while having a substantial impact on the interfacial electrostatic potential and the lateral mobility of the lipids. These effects are readily explained in terms of the arrangement that the amino-acids adopt when bound to the monolayer.
Fil: Klug, Joaquín. Universidad Nacional de Cuyo. Facultad de Ciencias Exactas y Naturales; Argentina. Queen's University Belfast; Reino Unido. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Masone, Diego Fernando. Universidad Nacional de Cuyo. Facultad de Ciencias Exactas y Naturales; Argentina. 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 Cienicas Médicas. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos; Argentina
Fil: del Popolo, Mario Gabriel. Universidad Nacional de Cuyo. Facultad de Ciencias Exactas y Naturales; Argentina
Materia
MOLECULAR DYNAMICS
LANGMUIR MONOLAYER
ARGININE
FREE ENERGY
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/49420
Acceder
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network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Molecular-level insight into the binding of arginine to a zwitterionic Langmuir monolayerKlug, JoaquínMasone, Diego Fernandodel Popolo, Mario GabrielMOLECULAR DYNAMICSLANGMUIR MONOLAYERARGININEFREE ENERGYhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Solutions of the cationic amino-acid arginine (Arg+) in contact with a phospholipid monolayer are investigated by molecular dynamics simulations. The results show that Arg+ binds strongly to the lipid/water interface, with adsorption free-energies ranging from -43.8 to -22.2 kJ mol-1, depending on the amino-acids concentration. The large binding energies are attributed to hydrogen bonding between the charged moieties Arg+ and the phosphate and carbonyl groups of the phospholipids, that compensate for changes in the levels of hydration upon adsorption. We show that a concentrated layer of Arg+, tightly bound to the interface, has little effect on the compression isotherm and the lateral mechanical properties of the monolayer, while having a substantial impact on the interfacial electrostatic potential and the lateral mobility of the lipids. These effects are readily explained in terms of the arrangement that the amino-acids adopt when bound to the monolayer.Fil: Klug, Joaquín. Universidad Nacional de Cuyo. Facultad de Ciencias Exactas y Naturales; Argentina. Queen's University Belfast; Reino Unido. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Masone, Diego Fernando. Universidad Nacional de Cuyo. Facultad de Ciencias Exactas y Naturales; Argentina. 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 Cienicas Médicas. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos; ArgentinaFil: del Popolo, Mario Gabriel. Universidad Nacional de Cuyo. Facultad de Ciencias Exactas y Naturales; ArgentinaRoyal Society of Chemistry2017-06info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/49420Klug, Joaquín; Masone, Diego Fernando; del Popolo, Mario Gabriel; Molecular-level insight into the binding of arginine to a zwitterionic Langmuir monolayer; Royal Society of Chemistry; RSC Advances; 7; 49; 6-2017; 30862-308692046-2069CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://xlink.rsc.org/?DOI=C7RA05359Binfo:eu-repo/semantics/altIdentifier/doi/10.1039/C7RA05359Binfo:eu-repo/semantics/altIdentifier/url/http://pubs.rsc.org/en/Content/ArticleLanding/2017/RA/C7RA05359B#!divAbstractinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:45:56Zoai:ri.conicet.gov.ar:11336/49420instacron: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:34982025-09-03 09:45:56.703CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Molecular-level insight into the binding of arginine to a zwitterionic Langmuir monolayer
title Molecular-level insight into the binding of arginine to a zwitterionic Langmuir monolayer
spellingShingle Molecular-level insight into the binding of arginine to a zwitterionic Langmuir monolayer
Klug, Joaquín
MOLECULAR DYNAMICS
LANGMUIR MONOLAYER
ARGININE
FREE ENERGY
title_short Molecular-level insight into the binding of arginine to a zwitterionic Langmuir monolayer
title_full Molecular-level insight into the binding of arginine to a zwitterionic Langmuir monolayer
title_fullStr Molecular-level insight into the binding of arginine to a zwitterionic Langmuir monolayer
title_full_unstemmed Molecular-level insight into the binding of arginine to a zwitterionic Langmuir monolayer
title_sort Molecular-level insight into the binding of arginine to a zwitterionic Langmuir monolayer
dc.creator.none.fl_str_mv Klug, Joaquín
Masone, Diego Fernando
del Popolo, Mario Gabriel
author Klug, Joaquín
author_facet Klug, Joaquín
Masone, Diego Fernando
del Popolo, Mario Gabriel
author_role author
author2 Masone, Diego Fernando
del Popolo, Mario Gabriel
author2_role author
author
dc.subject.none.fl_str_mv MOLECULAR DYNAMICS
LANGMUIR MONOLAYER
ARGININE
FREE ENERGY
topic MOLECULAR DYNAMICS
LANGMUIR MONOLAYER
ARGININE
FREE ENERGY
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Solutions of the cationic amino-acid arginine (Arg+) in contact with a phospholipid monolayer are investigated by molecular dynamics simulations. The results show that Arg+ binds strongly to the lipid/water interface, with adsorption free-energies ranging from -43.8 to -22.2 kJ mol-1, depending on the amino-acids concentration. The large binding energies are attributed to hydrogen bonding between the charged moieties Arg+ and the phosphate and carbonyl groups of the phospholipids, that compensate for changes in the levels of hydration upon adsorption. We show that a concentrated layer of Arg+, tightly bound to the interface, has little effect on the compression isotherm and the lateral mechanical properties of the monolayer, while having a substantial impact on the interfacial electrostatic potential and the lateral mobility of the lipids. These effects are readily explained in terms of the arrangement that the amino-acids adopt when bound to the monolayer.
Fil: Klug, Joaquín. Universidad Nacional de Cuyo. Facultad de Ciencias Exactas y Naturales; Argentina. Queen's University Belfast; Reino Unido. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Masone, Diego Fernando. Universidad Nacional de Cuyo. Facultad de Ciencias Exactas y Naturales; Argentina. 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 Cienicas Médicas. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos; Argentina
Fil: del Popolo, Mario Gabriel. Universidad Nacional de Cuyo. Facultad de Ciencias Exactas y Naturales; Argentina
description Solutions of the cationic amino-acid arginine (Arg+) in contact with a phospholipid monolayer are investigated by molecular dynamics simulations. The results show that Arg+ binds strongly to the lipid/water interface, with adsorption free-energies ranging from -43.8 to -22.2 kJ mol-1, depending on the amino-acids concentration. The large binding energies are attributed to hydrogen bonding between the charged moieties Arg+ and the phosphate and carbonyl groups of the phospholipids, that compensate for changes in the levels of hydration upon adsorption. We show that a concentrated layer of Arg+, tightly bound to the interface, has little effect on the compression isotherm and the lateral mechanical properties of the monolayer, while having a substantial impact on the interfacial electrostatic potential and the lateral mobility of the lipids. These effects are readily explained in terms of the arrangement that the amino-acids adopt when bound to the monolayer.
publishDate 2017
dc.date.none.fl_str_mv 2017-06
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/11336/49420
Klug, Joaquín; Masone, Diego Fernando; del Popolo, Mario Gabriel; Molecular-level insight into the binding of arginine to a zwitterionic Langmuir monolayer; Royal Society of Chemistry; RSC Advances; 7; 49; 6-2017; 30862-30869
2046-2069
CONICET Digital
CONICET
url http://hdl.handle.net/11336/49420
identifier_str_mv Klug, Joaquín; Masone, Diego Fernando; del Popolo, Mario Gabriel; Molecular-level insight into the binding of arginine to a zwitterionic Langmuir monolayer; Royal Society of Chemistry; RSC Advances; 7; 49; 6-2017; 30862-30869
2046-2069
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://xlink.rsc.org/?DOI=C7RA05359B
info:eu-repo/semantics/altIdentifier/doi/10.1039/C7RA05359B
info:eu-repo/semantics/altIdentifier/url/http://pubs.rsc.org/en/Content/ArticleLanding/2017/RA/C7RA05359B#!divAbstract
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Royal Society of Chemistry
publisher.none.fl_str_mv Royal Society of Chemistry
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 13.13397

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