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

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...

Descripción completa

Guardado en:
Detalles Bibliográficos
Autores principales: Zamarreño, Fernando, Herrera, Fernando E., Córsico, Betina, Costabel, Marcelo D.
Formato: Articulo
Lenguaje:Inglés
Publicado: 2012
Materias:
Bioquímica
Biomolecular modeling
Electrostatic interaction
Fatty acid binding protein
Molecular dynamics simulation
Protein-membrane interaction
Structure-function relation
Acceso en línea:http://sedici.unlp.edu.ar/handle/10915/84010
Aporte de:
SEDICI (UNLP) de Universidad Nacional de La Plata
id I19-R120-10915-84010
record_format dspace
institution Universidad Nacional de La Plata
institution_str I-19
repository_str R-120
collection SEDICI (UNLP)
language Inglés
topic Bioquímica
Biomolecular modeling
Electrostatic interaction
Fatty acid binding protein
Molecular dynamics simulation
Protein-membrane interaction
Structure-function relation
spellingShingle Bioquímica
Biomolecular modeling
Electrostatic interaction
Fatty acid binding protein
Molecular dynamics simulation
Protein-membrane interaction
Structure-function relation
Zamarreño, Fernando
Herrera, Fernando E.
Córsico, Betina
Costabel, Marcelo D.
Similar structures but different mechanisms: prediction of FABPs-membrane interaction by electrostatic calculation
topic_facet Bioquímica
Biomolecular modeling
Electrostatic interaction
Fatty acid binding protein
Molecular dynamics simulation
Protein-membrane interaction
Structure-function relation
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.
format Articulo
Articulo
author Zamarreño, Fernando
Herrera, Fernando E.
Córsico, Betina
Costabel, Marcelo D.
author_facet Zamarreño, Fernando
Herrera, Fernando E.
Córsico, Betina
Costabel, Marcelo D.
author_sort Zamarreño, Fernando
title Similar structures but different mechanisms: prediction of FABPs-membrane interaction by electrostatic calculation
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
publishDate 2012
url http://sedici.unlp.edu.ar/handle/10915/84010
work_keys_str_mv AT zamarrenofernando similarstructuresbutdifferentmechanismspredictionoffabpsmembraneinteractionbyelectrostaticcalculation
AT herrerafernandoe similarstructuresbutdifferentmechanismspredictionoffabpsmembraneinteractionbyelectrostaticcalculation
AT corsicobetina similarstructuresbutdifferentmechanismspredictionoffabpsmembraneinteractionbyelectrostaticcalculation
AT costabelmarcelod similarstructuresbutdifferentmechanismspredictionoffabpsmembraneinteractionbyelectrostaticcalculation
bdutipo_str Repositorios
_version_ 1764820488288206848

Ejemplares similares