Prediction of the most favorable configuration in the ACBP-membrane interaction based on electrostatic calculations

Acyl-CoA binding proteins (ACBPs) are highly conserved 10 kDa cytosolic proteins that bind medium- and long-chain acyl-CoA esters. They act as intracellular carriers of acyl-CoA and play a role in acyl-CoA metabolism, gene regulation, acyl-CoA-mediated cell signaling, transport-mediated lipid synthe...

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Detalles Bibliográficos
Autores: Vallejo, Diego, Zamarreño, Fernando, Guérin, Diego M.A., Grigera, José Raúl, Costabel, Marcelo D.
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2009
País:Argentina
Institución:Universidad Nacional de La Plata
Repositorio:SEDICI (UNLP)
Idioma:inglés
OAI Identifier:oai:sedici.unlp.edu.ar:10915/82670
Acceso en línea:http://sedici.unlp.edu.ar/handle/10915/82670
Access Level:acceso abierto
Palabra clave:Ciencias Astronómicas
ACBP
HgACBP
Protein-membrane interaction
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spelling Prediction of the most favorable configuration in the ACBP-membrane interaction based on electrostatic calculationsVallejo, DiegoZamarreño, FernandoGuérin, Diego M.A.Grigera, José RaúlCostabel, Marcelo D.Ciencias AstronómicasACBPHgACBPProtein-membrane interactionAcyl-CoA binding proteins (ACBPs) are highly conserved 10 kDa cytosolic proteins that bind medium- and long-chain acyl-CoA esters. They act as intracellular carriers of acyl-CoA and play a role in acyl-CoA metabolism, gene regulation, acyl-CoA-mediated cell signaling, transport-mediated lipid synthesis, membrane trafficking and also, ACBPs were indicated as a possible inhibitor of diazepam binding to the GABA-A receptor. To estimate the importance of the non-specific electrostatic energy in the ACBP-membrane interaction, we computationally modeled the interaction of HgACBP with both anionic and neutral membranes. To compute the Free Electrostatic Energy of Binding (dE), we used the Finite Difference Poisson Boltzmann Equation (FDPB) method as implemented in APBS. In the most energetically favorable orientation, ACBP brings charged residues Lys18 and Lys50 and hydrophobic residues Met46 and Leu47 into membrane surface proximity. This conformation suggests that these four ACBP amino acids are most likely to play a leading role in the ACBP-membrane interaction and ligand intake. Thus, we propose that long range electrostatic forces are the first step in the interaction mechanism between ACBP and membranes.Instituto de Física de Líquidos y Sistemas BiológicosFacultad de IngenieríaFacultad de Ciencias Exactas2009info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf696-700http://sedici.unlp.edu.ar/handle/10915/82670enginfo:eu-repo/semantics/altIdentifier/issn/0005-2736info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bbamem.2008.12.007info: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:UNLP2024-05-08T12:53:39Zoai:sedici.unlp.edu.ar:10915/82670Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292024-05-08 12:53:39.334SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv Prediction of the most favorable configuration in the ACBP-membrane interaction based on electrostatic calculations
title Prediction of the most favorable configuration in the ACBP-membrane interaction based on electrostatic calculations
spellingShingle Prediction of the most favorable configuration in the ACBP-membrane interaction based on electrostatic calculations
Vallejo, Diego
Ciencias Astronómicas
ACBP
HgACBP
Protein-membrane interaction
title_short Prediction of the most favorable configuration in the ACBP-membrane interaction based on electrostatic calculations
title_full Prediction of the most favorable configuration in the ACBP-membrane interaction based on electrostatic calculations
title_fullStr Prediction of the most favorable configuration in the ACBP-membrane interaction based on electrostatic calculations
title_full_unstemmed Prediction of the most favorable configuration in the ACBP-membrane interaction based on electrostatic calculations
title_sort Prediction of the most favorable configuration in the ACBP-membrane interaction based on electrostatic calculations
dc.creator.none.fl_str_mv Vallejo, Diego
Zamarreño, Fernando
Guérin, Diego M.A.
Grigera, José Raúl
Costabel, Marcelo D.
author Vallejo, Diego
author_facet Vallejo, Diego
Zamarreño, Fernando
Guérin, Diego M.A.
Grigera, José Raúl
Costabel, Marcelo D.
author_role author
author2 Zamarreño, Fernando
Guérin, Diego M.A.
Grigera, José Raúl
Costabel, Marcelo D.
author2_role author
author
author
author
dc.subject.none.fl_str_mv Ciencias Astronómicas
ACBP
HgACBP
Protein-membrane interaction
topic Ciencias Astronómicas
ACBP
HgACBP
Protein-membrane interaction
description Acyl-CoA binding proteins (ACBPs) are highly conserved 10 kDa cytosolic proteins that bind medium- and long-chain acyl-CoA esters. They act as intracellular carriers of acyl-CoA and play a role in acyl-CoA metabolism, gene regulation, acyl-CoA-mediated cell signaling, transport-mediated lipid synthesis, membrane trafficking and also, ACBPs were indicated as a possible inhibitor of diazepam binding to the GABA-A receptor. To estimate the importance of the non-specific electrostatic energy in the ACBP-membrane interaction, we computationally modeled the interaction of HgACBP with both anionic and neutral membranes. To compute the Free Electrostatic Energy of Binding (dE), we used the Finite Difference Poisson Boltzmann Equation (FDPB) method as implemented in APBS. In the most energetically favorable orientation, ACBP brings charged residues Lys18 and Lys50 and hydrophobic residues Met46 and Leu47 into membrane surface proximity. This conformation suggests that these four ACBP amino acids are most likely to play a leading role in the ACBP-membrane interaction and ligand intake. Thus, we propose that long range electrostatic forces are the first step in the interaction mechanism between ACBP and membranes.
publishDate 2009
dc.date.none.fl_str_mv 2009
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/10915/82670
url http://sedici.unlp.edu.ar/handle/10915/82670
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.2008.12.007
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
696-700
dc.source.none.fl_str_mv reponame:SEDICI (UNLP)
instname:Universidad Nacional de La Plata
instacron:UNLP
instname_str Universidad Nacional de La Plata
instacron_str UNLP
institution UNLP
reponame_str SEDICI (UNLP)
collection SEDICI (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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score 15,811543

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