Prediction of the most favorable configuration in the ACBP-membrane interaction based on electrostatic calculations
- Autores
- Vallejo, Diego; Zamarreño, Fernando; Guérin, Diego M.A.; Grigera, José Raúl; Costabel, Marcelo D.
- Año de publicación
- 2009
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- 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.
Instituto de Física de Líquidos y Sistemas Biológicos
Facultad de Ingeniería
Facultad de Ciencias Exactas - Materia
-
Ciencias Astronómicas
ACBP
HgACBP
Protein-membrane interaction - 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:10915/82670
Ver los metadatos del registro completo
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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:UNLP2025-09-29T11:15:36Zoai: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:13292025-09-29 11:15:36.383SEDICI (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 |
dc.description.none.fl_txt_mv |
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. Instituto de Física de Líquidos y Sistemas Biológicos Facultad de Ingeniería Facultad de Ciencias Exactas |
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 |
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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 |
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SEDICI (UNLP) - Universidad Nacional de La Plata |
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