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
- Institución
- Universidad Nacional de La Plata
- OAI Identificador
- oai:sedici.unlp.edu.ar:10915/84010
Ver los metadatos del registro completo
id |
SEDICI_820cc6e20c5e31be06958f06fce062bc |
---|---|
oai_identifier_str |
oai:sedici.unlp.edu.ar:10915/84010 |
network_acronym_str |
SEDICI |
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) |
collection |
SEDICI (UNLP) |
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 |
_version_ |
1844616032791035904 |
score |
13.070432 |