Evaluation of the Defay-Prigogine model for the membrane interphase in relation to biological response in membrane-protein interactions

Autores
Disalvo, Edgardo Anibal; Hollmann, Axel; Semorile, Liliana Carmen; Martini, María Florencia
Año de publicación
2013
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Surface water activity appears as a common factor when the interaction of several aqueous soluble and surface active proteins with lipid membranes of different composition is measured by the changes in surface pressure of a lipid monolayer. The perturbation of the lipid surface caused by aqueous soluble proteins depends on the composition of the hydrocarbon phases, either modified by unsaturated bonds in the acyl chains or by inclusion of cholesterol. The cut-off (critical) surface pressure in monolayers, at which no effect of the proteins is found, is related to the composition of the head group region. The perturbation of surface pressure is produced by proteins when the area per lipid is above just 4% larger than that corresponding to the hydration shell of the phospholipid head groups found in the cut -off. This area excess gives place to regions in which the chemical potential of water changes with respect to bulk water. According to the Defay-Prigogine relation this interfacial water activity is the reason of the surface pressure increase induced by aqueous soluble proteins injected in the subphase. As predicted by solution chemistry, the increase of surface pressure is independent of the protein nature but depends on the water surface state determined by the lipid composition.
Fil: Disalvo, Edgardo Anibal. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro de Investigaciones y Transferencia de Santiago del Estero; Argentina
Fil: Hollmann, Axel. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnologia. Laboratorio de Microbiologia Molecular; . Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Química Analítica y Fisicoquímica. Cátedra de Química General e Inorgánica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro de Investigaciones y Transferencia de Santiago del Estero; Argentina
Fil: Semorile, Liliana Carmen. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Laboratorio de Microbiología Molecular; Argentina
Fil: Martini, María Florencia. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Tecnología Farmacéutica; Argentina
Materia
Lipid Membranes
Water-Membrane Interphases
Protein Interaction
Interfacial Water Activity
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:11336/1774
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/1774
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Evaluation of the Defay-Prigogine model for the membrane interphase in relation to biological response in membrane-protein interactionsDisalvo, Edgardo AnibalHollmann, AxelSemorile, Liliana CarmenMartini, María FlorenciaLipid MembranesWater-Membrane InterphasesProtein InteractionInterfacial Water Activityhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Surface water activity appears as a common factor when the interaction of several aqueous soluble and surface active proteins with lipid membranes of different composition is measured by the changes in surface pressure of a lipid monolayer. The perturbation of the lipid surface caused by aqueous soluble proteins depends on the composition of the hydrocarbon phases, either modified by unsaturated bonds in the acyl chains or by inclusion of cholesterol. The cut-off (critical) surface pressure in monolayers, at which no effect of the proteins is found, is related to the composition of the head group region. The perturbation of surface pressure is produced by proteins when the area per lipid is above just 4% larger than that corresponding to the hydration shell of the phospholipid head groups found in the cut -off. This area excess gives place to regions in which the chemical potential of water changes with respect to bulk water. According to the Defay-Prigogine relation this interfacial water activity is the reason of the surface pressure increase induced by aqueous soluble proteins injected in the subphase. As predicted by solution chemistry, the increase of surface pressure is independent of the protein nature but depends on the water surface state determined by the lipid composition.Fil: Disalvo, Edgardo Anibal. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro de Investigaciones y Transferencia de Santiago del Estero; ArgentinaFil: Hollmann, Axel. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnologia. Laboratorio de Microbiologia Molecular; . Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Química Analítica y Fisicoquímica. Cátedra de Química General e Inorgánica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro de Investigaciones y Transferencia de Santiago del Estero; ArgentinaFil: Semorile, Liliana Carmen. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Laboratorio de Microbiología Molecular; ArgentinaFil: Martini, María Florencia. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Tecnología Farmacéutica; ArgentinaElsevier2013-07info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/1774Disalvo, Edgardo Anibal; Hollmann, Axel; Semorile, Liliana Carmen; Martini, María Florencia; Evaluation of the Defay-Prigogine model for the membrane interphase in relation to biological response in membrane-protein interactions; Elsevier; Biochimica et Biophysica Acta - Biomembranes; 1828; 8; 7-2013; 1834-18390005-2736enginfo:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0005273613000953info:eu-repo/semantics/altIdentifier/doi/doi:10.1016/j.bbamem.2013.03.026info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T11:38:32Zoai:ri.conicet.gov.ar:11336/1774instacron: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 11:38:32.433CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Evaluation of the Defay-Prigogine model for the membrane interphase in relation to biological response in membrane-protein interactions
title Evaluation of the Defay-Prigogine model for the membrane interphase in relation to biological response in membrane-protein interactions
spellingShingle Evaluation of the Defay-Prigogine model for the membrane interphase in relation to biological response in membrane-protein interactions
Disalvo, Edgardo Anibal
Lipid Membranes
Water-Membrane Interphases
Protein Interaction
Interfacial Water Activity
title_short Evaluation of the Defay-Prigogine model for the membrane interphase in relation to biological response in membrane-protein interactions
title_full Evaluation of the Defay-Prigogine model for the membrane interphase in relation to biological response in membrane-protein interactions
title_fullStr Evaluation of the Defay-Prigogine model for the membrane interphase in relation to biological response in membrane-protein interactions
title_full_unstemmed Evaluation of the Defay-Prigogine model for the membrane interphase in relation to biological response in membrane-protein interactions
title_sort Evaluation of the Defay-Prigogine model for the membrane interphase in relation to biological response in membrane-protein interactions
dc.creator.none.fl_str_mv Disalvo, Edgardo Anibal
Hollmann, Axel
Semorile, Liliana Carmen
Martini, María Florencia
author Disalvo, Edgardo Anibal
author_facet Disalvo, Edgardo Anibal
Hollmann, Axel
Semorile, Liliana Carmen
Martini, María Florencia
author_role author
author2 Hollmann, Axel
Semorile, Liliana Carmen
Martini, María Florencia
author2_role author
author
author
dc.subject.none.fl_str_mv Lipid Membranes
Water-Membrane Interphases
Protein Interaction
Interfacial Water Activity
topic Lipid Membranes
Water-Membrane Interphases
Protein Interaction
Interfacial Water Activity
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Surface water activity appears as a common factor when the interaction of several aqueous soluble and surface active proteins with lipid membranes of different composition is measured by the changes in surface pressure of a lipid monolayer. The perturbation of the lipid surface caused by aqueous soluble proteins depends on the composition of the hydrocarbon phases, either modified by unsaturated bonds in the acyl chains or by inclusion of cholesterol. The cut-off (critical) surface pressure in monolayers, at which no effect of the proteins is found, is related to the composition of the head group region. The perturbation of surface pressure is produced by proteins when the area per lipid is above just 4% larger than that corresponding to the hydration shell of the phospholipid head groups found in the cut -off. This area excess gives place to regions in which the chemical potential of water changes with respect to bulk water. According to the Defay-Prigogine relation this interfacial water activity is the reason of the surface pressure increase induced by aqueous soluble proteins injected in the subphase. As predicted by solution chemistry, the increase of surface pressure is independent of the protein nature but depends on the water surface state determined by the lipid composition.
Fil: Disalvo, Edgardo Anibal. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro de Investigaciones y Transferencia de Santiago del Estero; Argentina
Fil: Hollmann, Axel. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnologia. Laboratorio de Microbiologia Molecular; . Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Química Analítica y Fisicoquímica. Cátedra de Química General e Inorgánica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro de Investigaciones y Transferencia de Santiago del Estero; Argentina
Fil: Semorile, Liliana Carmen. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Laboratorio de Microbiología Molecular; Argentina
Fil: Martini, María Florencia. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Tecnología Farmacéutica; Argentina
description Surface water activity appears as a common factor when the interaction of several aqueous soluble and surface active proteins with lipid membranes of different composition is measured by the changes in surface pressure of a lipid monolayer. The perturbation of the lipid surface caused by aqueous soluble proteins depends on the composition of the hydrocarbon phases, either modified by unsaturated bonds in the acyl chains or by inclusion of cholesterol. The cut-off (critical) surface pressure in monolayers, at which no effect of the proteins is found, is related to the composition of the head group region. The perturbation of surface pressure is produced by proteins when the area per lipid is above just 4% larger than that corresponding to the hydration shell of the phospholipid head groups found in the cut -off. This area excess gives place to regions in which the chemical potential of water changes with respect to bulk water. According to the Defay-Prigogine relation this interfacial water activity is the reason of the surface pressure increase induced by aqueous soluble proteins injected in the subphase. As predicted by solution chemistry, the increase of surface pressure is independent of the protein nature but depends on the water surface state determined by the lipid composition.
publishDate 2013
dc.date.none.fl_str_mv 2013-07
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/11336/1774
Disalvo, Edgardo Anibal; Hollmann, Axel; Semorile, Liliana Carmen; Martini, María Florencia; Evaluation of the Defay-Prigogine model for the membrane interphase in relation to biological response in membrane-protein interactions; Elsevier; Biochimica et Biophysica Acta - Biomembranes; 1828; 8; 7-2013; 1834-1839
0005-2736
url http://hdl.handle.net/11336/1774
identifier_str_mv Disalvo, Edgardo Anibal; Hollmann, Axel; Semorile, Liliana Carmen; Martini, María Florencia; Evaluation of the Defay-Prigogine model for the membrane interphase in relation to biological response in membrane-protein interactions; Elsevier; Biochimica et Biophysica Acta - Biomembranes; 1828; 8; 7-2013; 1834-1839
0005-2736
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0005273613000953
info:eu-repo/semantics/altIdentifier/doi/doi:10.1016/j.bbamem.2013.03.026
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
publisher.none.fl_str_mv Elsevier
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_ 1846782042833944576
score 12.982451

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