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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/1774
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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 Técnicas2025-09-29T10:08:42Zoai: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:34982025-09-29 10:08:43.179CONICET 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_ |
1844613957647597568 |
score |
13.070432 |