Interactions of the fatty acid-binding protein ReP1-NCXSQ with lipidmembranes. Influence of the membrane electricfield on bindingand orientation

Autores
Galassi, Vanesa Viviana; Villarreal, Marcos Ariel; Posada, Velia Lucy; Montich, Guillermo Gabriel
Año de publicación
2014
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The regulatory protein of the squid nerve sodium calcium exchanger (ReP1-NCXSQ) is a 15 kDa soluble, intracel-lular proteinthatregulates the activity ofthe Na+/Ca2+exchanger inthe squidaxon. It isa member of thecellularretinoic acid-binding proteins family and the fatty acid-binding proteins superfamily. It is composed of ten betastrands defining an inner cavity and a domain of two short alpha helix segments. In this work, we studied thebinding and orientation of ReP1-NCXSQ in anionic and zwitterionic lipid membranes using molecular dynamics(MD) simulations. Binding to lipid membranes was also measured byfiltration binding assay. ReP1-NCXSQ ac-quired an orientation in the anionic membranes with the positive end of the macrodipole pointing to the lipidmembrane. Potential of mean force calculations, in agreement with experimental measurements, showed thatthe binding to the anionic interfaces in low ionic strength was stronger than the binding to anionic interfacesin high ionic strength or to zwitterionic membranes. The results of MD showed that the electrostatic bindingcan be mediated not only by defined patches or domains of basic residues but also by a global asymmetric distri-bution of charges. A combination of dipole–electricfield interaction and local interactions determined theorientation of ReP1-NCXSQ in the interface.
Fil: Galassi, Vanesa Viviana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
Fil: Villarreal, Marcos Ariel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones en Físico-química de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Instituto de Investigaciones en Físico-química de Córdoba; Argentina
Fil: Posada, Velia Lucy. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
Fil: Montich, Guillermo Gabriel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
Materia
Rep1-Ncxsq
Lipid Membrane
Binding
Orientation
Molecular Dynamics
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:11336/31503
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/31503
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Interactions of the fatty acid-binding protein ReP1-NCXSQ with lipidmembranes. Influence of the membrane electricfield on bindingand orientationGalassi, Vanesa VivianaVillarreal, Marcos ArielPosada, Velia LucyMontich, Guillermo GabrielRep1-NcxsqLipid MembraneBindingOrientationMolecular Dynamicshttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The regulatory protein of the squid nerve sodium calcium exchanger (ReP1-NCXSQ) is a 15 kDa soluble, intracel-lular proteinthatregulates the activity ofthe Na+/Ca2+exchanger inthe squidaxon. It isa member of thecellularretinoic acid-binding proteins family and the fatty acid-binding proteins superfamily. It is composed of ten betastrands defining an inner cavity and a domain of two short alpha helix segments. In this work, we studied thebinding and orientation of ReP1-NCXSQ in anionic and zwitterionic lipid membranes using molecular dynamics(MD) simulations. Binding to lipid membranes was also measured byfiltration binding assay. ReP1-NCXSQ ac-quired an orientation in the anionic membranes with the positive end of the macrodipole pointing to the lipidmembrane. Potential of mean force calculations, in agreement with experimental measurements, showed thatthe binding to the anionic interfaces in low ionic strength was stronger than the binding to anionic interfacesin high ionic strength or to zwitterionic membranes. The results of MD showed that the electrostatic bindingcan be mediated not only by defined patches or domains of basic residues but also by a global asymmetric distri-bution of charges. A combination of dipole–electricfield interaction and local interactions determined theorientation of ReP1-NCXSQ in the interface.Fil: Galassi, Vanesa Viviana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; ArgentinaFil: Villarreal, Marcos Ariel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones en Físico-química de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Instituto de Investigaciones en Físico-química de Córdoba; ArgentinaFil: Posada, Velia Lucy. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; ArgentinaFil: Montich, Guillermo Gabriel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; ArgentinaElsevier Science2014-03info: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/11336/31503Montich, Guillermo Gabriel; Posada, Velia Lucy; Villarreal, Marcos Ariel; Galassi, Vanesa Viviana; Interactions of the fatty acid-binding protein ReP1-NCXSQ with lipidmembranes. Influence of the membrane electricfield on bindingand orientation; Elsevier Science; Biochimica et Biophysica Acta - Biomembranes; 1838; 3; 3-2014; 910-9200005-2736CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.bbamem.2013.11.008info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0005273613004057info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T11:02:50Zoai:ri.conicet.gov.ar:11336/31503instacron: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 11:02:51.219CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Interactions of the fatty acid-binding protein ReP1-NCXSQ with lipidmembranes. Influence of the membrane electricfield on bindingand orientation
title Interactions of the fatty acid-binding protein ReP1-NCXSQ with lipidmembranes. Influence of the membrane electricfield on bindingand orientation
spellingShingle Interactions of the fatty acid-binding protein ReP1-NCXSQ with lipidmembranes. Influence of the membrane electricfield on bindingand orientation
Galassi, Vanesa Viviana
Rep1-Ncxsq
Lipid Membrane
Binding
Orientation
Molecular Dynamics
title_short Interactions of the fatty acid-binding protein ReP1-NCXSQ with lipidmembranes. Influence of the membrane electricfield on bindingand orientation
title_full Interactions of the fatty acid-binding protein ReP1-NCXSQ with lipidmembranes. Influence of the membrane electricfield on bindingand orientation
title_fullStr Interactions of the fatty acid-binding protein ReP1-NCXSQ with lipidmembranes. Influence of the membrane electricfield on bindingand orientation
title_full_unstemmed Interactions of the fatty acid-binding protein ReP1-NCXSQ with lipidmembranes. Influence of the membrane electricfield on bindingand orientation
title_sort Interactions of the fatty acid-binding protein ReP1-NCXSQ with lipidmembranes. Influence of the membrane electricfield on bindingand orientation
dc.creator.none.fl_str_mv Galassi, Vanesa Viviana
Villarreal, Marcos Ariel
Posada, Velia Lucy
Montich, Guillermo Gabriel
author Galassi, Vanesa Viviana
author_facet Galassi, Vanesa Viviana
Villarreal, Marcos Ariel
Posada, Velia Lucy
Montich, Guillermo Gabriel
author_role author
author2 Villarreal, Marcos Ariel
Posada, Velia Lucy
Montich, Guillermo Gabriel
author2_role author
author
author
dc.subject.none.fl_str_mv Rep1-Ncxsq
Lipid Membrane
Binding
Orientation
Molecular Dynamics
topic Rep1-Ncxsq
Lipid Membrane
Binding
Orientation
Molecular Dynamics
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 regulatory protein of the squid nerve sodium calcium exchanger (ReP1-NCXSQ) is a 15 kDa soluble, intracel-lular proteinthatregulates the activity ofthe Na+/Ca2+exchanger inthe squidaxon. It isa member of thecellularretinoic acid-binding proteins family and the fatty acid-binding proteins superfamily. It is composed of ten betastrands defining an inner cavity and a domain of two short alpha helix segments. In this work, we studied thebinding and orientation of ReP1-NCXSQ in anionic and zwitterionic lipid membranes using molecular dynamics(MD) simulations. Binding to lipid membranes was also measured byfiltration binding assay. ReP1-NCXSQ ac-quired an orientation in the anionic membranes with the positive end of the macrodipole pointing to the lipidmembrane. Potential of mean force calculations, in agreement with experimental measurements, showed thatthe binding to the anionic interfaces in low ionic strength was stronger than the binding to anionic interfacesin high ionic strength or to zwitterionic membranes. The results of MD showed that the electrostatic bindingcan be mediated not only by defined patches or domains of basic residues but also by a global asymmetric distri-bution of charges. A combination of dipole–electricfield interaction and local interactions determined theorientation of ReP1-NCXSQ in the interface.
Fil: Galassi, Vanesa Viviana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
Fil: Villarreal, Marcos Ariel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones en Físico-química de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Instituto de Investigaciones en Físico-química de Córdoba; Argentina
Fil: Posada, Velia Lucy. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
Fil: Montich, Guillermo Gabriel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
description The regulatory protein of the squid nerve sodium calcium exchanger (ReP1-NCXSQ) is a 15 kDa soluble, intracel-lular proteinthatregulates the activity ofthe Na+/Ca2+exchanger inthe squidaxon. It isa member of thecellularretinoic acid-binding proteins family and the fatty acid-binding proteins superfamily. It is composed of ten betastrands defining an inner cavity and a domain of two short alpha helix segments. In this work, we studied thebinding and orientation of ReP1-NCXSQ in anionic and zwitterionic lipid membranes using molecular dynamics(MD) simulations. Binding to lipid membranes was also measured byfiltration binding assay. ReP1-NCXSQ ac-quired an orientation in the anionic membranes with the positive end of the macrodipole pointing to the lipidmembrane. Potential of mean force calculations, in agreement with experimental measurements, showed thatthe binding to the anionic interfaces in low ionic strength was stronger than the binding to anionic interfacesin high ionic strength or to zwitterionic membranes. The results of MD showed that the electrostatic bindingcan be mediated not only by defined patches or domains of basic residues but also by a global asymmetric distri-bution of charges. A combination of dipole–electricfield interaction and local interactions determined theorientation of ReP1-NCXSQ in the interface.
publishDate 2014
dc.date.none.fl_str_mv 2014-03
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/11336/31503
Montich, Guillermo Gabriel; Posada, Velia Lucy; Villarreal, Marcos Ariel; Galassi, Vanesa Viviana; Interactions of the fatty acid-binding protein ReP1-NCXSQ with lipidmembranes. Influence of the membrane electricfield on bindingand orientation; Elsevier Science; Biochimica et Biophysica Acta - Biomembranes; 1838; 3; 3-2014; 910-920
0005-2736
CONICET Digital
CONICET
url http://hdl.handle.net/11336/31503
identifier_str_mv Montich, Guillermo Gabriel; Posada, Velia Lucy; Villarreal, Marcos Ariel; Galassi, Vanesa Viviana; Interactions of the fatty acid-binding protein ReP1-NCXSQ with lipidmembranes. Influence of the membrane electricfield on bindingand orientation; Elsevier Science; Biochimica et Biophysica Acta - Biomembranes; 1838; 3; 3-2014; 910-920
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/doi/10.1016/j.bbamem.2013.11.008
info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0005273613004057
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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score 12.982451

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