Similar structures but different mechanisms: Prediction of FABPs-membrane interaction by electrostatic calculation

Autores
Zamarreño, Fernando; Herrera, Fernando Enrique; Córsico, Betina; Costabel, Marcelo Daniel
Año de publicación
2012
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The role of fatty acid binding proteins as intracellular fatty acid transporters may require their direct interaction with membranes. In this way different mechanisms have been previously characterized through experimental studies suggesting different models for FABPs-membrane association, although the process in which the molecule adsorbs to the membrane remains to be elucidated. To estimate the importance of the electrostatic energy in the FABP-membrane interaction, we computationally modeled the interaction of different FABPs with both anionic and neutral membranes. Free Electrostatic Energy of Binding (dE), was computed using Finite Difference Poisson Boltzmann Equation (FDPB) method as implemented in APBS (Adaptive Poisson Boltzmann Solver). Based on the computational analysis, it is found that recruitment to membranes is facilitated by non-specific electrostatic interactions. Also energetic analysis can quantitatively differentiate among the mechanisms of membrane association proposed and determinate the most energetically favorable configuration for the membrane-associated states of different FABPs. This type of calculations could provide a starting point for further computational or experimental analysis.
Fil: Zamarreño, Fernando. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional del Sur. Departamento de Física; Argentina
Fil: Herrera, Fernando Enrique. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas; Argentina
Fil: Córsico, Betina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner". Universidad Nacional de la Plata. Facultad de Ciencias Médicas. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner"; Argentina
Fil: Costabel, Marcelo Daniel. Universidad Nacional del Sur. Departamento de Física; Argentina
Materia
Biomolecular Modeling
Electrostatic Interaction
Fatty Acid Binding Protein
Molecular Dynamics Simulation
Protein-Membrane Interaction
Structure-Function Relation
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:11336/82290
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/82290
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Similar structures but different mechanisms: Prediction of FABPs-membrane interaction by electrostatic calculationZamarreño, FernandoHerrera, Fernando EnriqueCórsico, BetinaCostabel, Marcelo DanielBiomolecular ModelingElectrostatic InteractionFatty Acid Binding ProteinMolecular Dynamics SimulationProtein-Membrane InteractionStructure-Function RelationThe role of fatty acid binding proteins as intracellular fatty acid transporters may require their direct interaction with membranes. In this way different mechanisms have been previously characterized through experimental studies suggesting different models for FABPs-membrane association, although the process in which the molecule adsorbs to the membrane remains to be elucidated. To estimate the importance of the electrostatic energy in the FABP-membrane interaction, we computationally modeled the interaction of different FABPs with both anionic and neutral membranes. Free Electrostatic Energy of Binding (dE), was computed using Finite Difference Poisson Boltzmann Equation (FDPB) method as implemented in APBS (Adaptive Poisson Boltzmann Solver). Based on the computational analysis, it is found that recruitment to membranes is facilitated by non-specific electrostatic interactions. Also energetic analysis can quantitatively differentiate among the mechanisms of membrane association proposed and determinate the most energetically favorable configuration for the membrane-associated states of different FABPs. This type of calculations could provide a starting point for further computational or experimental analysis.Fil: Zamarreño, Fernando. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional del Sur. Departamento de Física; ArgentinaFil: Herrera, Fernando Enrique. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas; ArgentinaFil: Córsico, Betina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner". Universidad Nacional de la Plata. Facultad de Ciencias Médicas. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner"; ArgentinaFil: Costabel, Marcelo Daniel. Universidad Nacional del Sur. Departamento de Física; ArgentinaElsevier Science2012-07info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/82290Zamarreño, Fernando; Herrera, Fernando Enrique; Córsico, Betina; Costabel, Marcelo Daniel; Similar structures but different mechanisms: Prediction of FABPs-membrane interaction by electrostatic calculation; Elsevier Science; Biochimica et Biophysica Acta - Biomembranes; 1818; 7; 7-2012; 1691-16970005-2736CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0005273612000831info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bbamem.2012.03.003info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:41:31Zoai:ri.conicet.gov.ar:11336/82290instacron: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 10:41:31.322CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Similar structures but different mechanisms: Prediction of FABPs-membrane interaction by electrostatic calculation
title Similar structures but different mechanisms: Prediction of FABPs-membrane interaction by electrostatic calculation
spellingShingle Similar structures but different mechanisms: Prediction of FABPs-membrane interaction by electrostatic calculation
Zamarreño, Fernando
Biomolecular Modeling
Electrostatic Interaction
Fatty Acid Binding Protein
Molecular Dynamics Simulation
Protein-Membrane Interaction
Structure-Function Relation
title_short Similar structures but different mechanisms: Prediction of FABPs-membrane interaction by electrostatic calculation
title_full Similar structures but different mechanisms: Prediction of FABPs-membrane interaction by electrostatic calculation
title_fullStr Similar structures but different mechanisms: Prediction of FABPs-membrane interaction by electrostatic calculation
title_full_unstemmed Similar structures but different mechanisms: Prediction of FABPs-membrane interaction by electrostatic calculation
title_sort Similar structures but different mechanisms: Prediction of FABPs-membrane interaction by electrostatic calculation
dc.creator.none.fl_str_mv Zamarreño, Fernando
Herrera, Fernando Enrique
Córsico, Betina
Costabel, Marcelo Daniel
author Zamarreño, Fernando
author_facet Zamarreño, Fernando
Herrera, Fernando Enrique
Córsico, Betina
Costabel, Marcelo Daniel
author_role author
author2 Herrera, Fernando Enrique
Córsico, Betina
Costabel, Marcelo Daniel
author2_role author
author
author
dc.subject.none.fl_str_mv Biomolecular Modeling
Electrostatic Interaction
Fatty Acid Binding Protein
Molecular Dynamics Simulation
Protein-Membrane Interaction
Structure-Function Relation
topic Biomolecular Modeling
Electrostatic Interaction
Fatty Acid Binding Protein
Molecular Dynamics Simulation
Protein-Membrane Interaction
Structure-Function Relation
dc.description.none.fl_txt_mv The role of fatty acid binding proteins as intracellular fatty acid transporters may require their direct interaction with membranes. In this way different mechanisms have been previously characterized through experimental studies suggesting different models for FABPs-membrane association, although the process in which the molecule adsorbs to the membrane remains to be elucidated. To estimate the importance of the electrostatic energy in the FABP-membrane interaction, we computationally modeled the interaction of different FABPs with both anionic and neutral membranes. Free Electrostatic Energy of Binding (dE), was computed using Finite Difference Poisson Boltzmann Equation (FDPB) method as implemented in APBS (Adaptive Poisson Boltzmann Solver). Based on the computational analysis, it is found that recruitment to membranes is facilitated by non-specific electrostatic interactions. Also energetic analysis can quantitatively differentiate among the mechanisms of membrane association proposed and determinate the most energetically favorable configuration for the membrane-associated states of different FABPs. This type of calculations could provide a starting point for further computational or experimental analysis.
Fil: Zamarreño, Fernando. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional del Sur. Departamento de Física; Argentina
Fil: Herrera, Fernando Enrique. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas; Argentina
Fil: Córsico, Betina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner". Universidad Nacional de la Plata. Facultad de Ciencias Médicas. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner"; Argentina
Fil: Costabel, Marcelo Daniel. Universidad Nacional del Sur. Departamento de Física; Argentina
description The role of fatty acid binding proteins as intracellular fatty acid transporters may require their direct interaction with membranes. In this way different mechanisms have been previously characterized through experimental studies suggesting different models for FABPs-membrane association, although the process in which the molecule adsorbs to the membrane remains to be elucidated. To estimate the importance of the electrostatic energy in the FABP-membrane interaction, we computationally modeled the interaction of different FABPs with both anionic and neutral membranes. Free Electrostatic Energy of Binding (dE), was computed using Finite Difference Poisson Boltzmann Equation (FDPB) method as implemented in APBS (Adaptive Poisson Boltzmann Solver). Based on the computational analysis, it is found that recruitment to membranes is facilitated by non-specific electrostatic interactions. Also energetic analysis can quantitatively differentiate among the mechanisms of membrane association proposed and determinate the most energetically favorable configuration for the membrane-associated states of different FABPs. This type of calculations could provide a starting point for further computational or experimental analysis.
publishDate 2012
dc.date.none.fl_str_mv 2012-07
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/11336/82290
Zamarreño, Fernando; Herrera, Fernando Enrique; Córsico, Betina; Costabel, Marcelo Daniel; Similar structures but different mechanisms: Prediction of FABPs-membrane interaction by electrostatic calculation; Elsevier Science; Biochimica et Biophysica Acta - Biomembranes; 1818; 7; 7-2012; 1691-1697
0005-2736
CONICET Digital
CONICET
url http://hdl.handle.net/11336/82290
identifier_str_mv Zamarreño, Fernando; Herrera, Fernando Enrique; Córsico, Betina; Costabel, Marcelo Daniel; Similar structures but different mechanisms: Prediction of FABPs-membrane interaction by electrostatic calculation; Elsevier Science; Biochimica et Biophysica Acta - Biomembranes; 1818; 7; 7-2012; 1691-1697
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/http://www.sciencedirect.com/science/article/pii/S0005273612000831
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bbamem.2012.03.003
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
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 13.070432

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