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

Autores
Zamarreño, Fernando; Herrera, Fernando E.; Córsico, Betina; Costabel, Marcelo D.
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.
Instituto de Investigaciones Bioquímicas de La Plata
Materia
Bioquímica
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
http://creativecommons.org/licenses/by-nc-sa/4.0/
Repositorio
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/84010

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repository_id_str 1329
network_name_str SEDICI (UNLP)
spelling Similar structures but different mechanisms: prediction of FABPs-membrane interaction by electrostatic calculationZamarreño, FernandoHerrera, Fernando E.Córsico, BetinaCostabel, Marcelo D.BioquímicaBiomolecular 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.Instituto de Investigaciones Bioquímicas de La Plata2012info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf1691-1697http://sedici.unlp.edu.ar/handle/10915/84010enginfo:eu-repo/semantics/altIdentifier/issn/0005-2736info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bbamem.2012.03.003info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-sa/4.0/Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-09-29T11:16:01Zoai:sedici.unlp.edu.ar:10915/84010Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-29 11:16:01.67SEDICI (UNLP) - Universidad Nacional de La Platafalse
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
Bioquímica
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 E.
Córsico, Betina
Costabel, Marcelo D.
author Zamarreño, Fernando
author_facet Zamarreño, Fernando
Herrera, Fernando E.
Córsico, Betina
Costabel, Marcelo D.
author_role author
author2 Herrera, Fernando E.
Córsico, Betina
Costabel, Marcelo D.
author2_role author
author
author
dc.subject.none.fl_str_mv Bioquímica
Biomolecular modeling
Electrostatic interaction
Fatty acid binding protein
Molecular dynamics simulation
Protein-membrane interaction
Structure-function relation
topic Bioquímica
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.
Instituto de Investigaciones Bioquímicas de La Plata
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
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
Articulo
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://sedici.unlp.edu.ar/handle/10915/84010
url http://sedici.unlp.edu.ar/handle/10915/84010
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/issn/0005-2736
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bbamem.2012.03.003
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
dc.format.none.fl_str_mv application/pdf
1691-1697
dc.source.none.fl_str_mv reponame:SEDICI (UNLP)
instname:Universidad Nacional de La Plata
instacron:UNLP
reponame_str SEDICI (UNLP)
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instname_str Universidad Nacional de La Plata
instacron_str UNLP
institution UNLP
repository.name.fl_str_mv SEDICI (UNLP) - Universidad Nacional de La Plata
repository.mail.fl_str_mv alira@sedici.unlp.edu.ar
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