Conserved charged amino acids are key determinants for fatty acid binding proteins (FABPs)-membrane interactions : A multi-methodological computational approach

Based on the analysis of the mechanism of ligand transfer to membranes employing in vitro methods, Fatty Acid Binding Protein (FABP) family has been divided in two subgroups: collisional and diffusional FABPs. Although the collisional mechanism has been well characterized employing in vitro methods,...

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Autores principales: Zamarreño, Fernando, Giorgetti, Alejandro, Amundarain, María Julia, Viso, Juan Francisco, Córsico, Betina, Costabel, Marcelo Daniel
Formato: Articulo
Lenguaje:Inglés
Publicado: 2017
Materias:
Ciencias Exactas
Ciencias Médicas
fatty acid binding protein
electrostatic interaction
molecular dynamics
protein–membrane interaction
Acceso en línea:http://sedici.unlp.edu.ar/handle/10915/148171
Aporte de:
SEDICI (UNLP) de Universidad Nacional de La Plata
id I19-R120-10915-148171
record_format dspace
institution Universidad Nacional de La Plata
institution_str I-19
repository_str R-120
collection SEDICI (UNLP)
language Inglés
topic Ciencias Exactas
Ciencias Médicas
fatty acid binding protein
electrostatic interaction
molecular dynamics
protein–membrane interaction
spellingShingle Ciencias Exactas
Ciencias Médicas
fatty acid binding protein
electrostatic interaction
molecular dynamics
protein–membrane interaction
Zamarreño, Fernando
Giorgetti, Alejandro
Amundarain, María Julia
Viso, Juan Francisco
Córsico, Betina
Costabel, Marcelo Daniel
Conserved charged amino acids are key determinants for fatty acid binding proteins (FABPs)-membrane interactions : A multi-methodological computational approach
topic_facet Ciencias Exactas
Ciencias Médicas
fatty acid binding protein
electrostatic interaction
molecular dynamics
protein–membrane interaction
description Based on the analysis of the mechanism of ligand transfer to membranes employing in vitro methods, Fatty Acid Binding Protein (FABP) family has been divided in two subgroups: collisional and diffusional FABPs. Although the collisional mechanism has been well characterized employing in vitro methods, the structural features responsible for the difference between collisional and diffusional mechanisms remain uncertain. In this work, we have identified the amino acids putatively responsible for the interaction with membranes of both, collisional and diffusional, subgroups of FABPs. Moreover, we show how specific changes in FABPs’ structure could change the mechanism of interaction with membranes. We have computed protein–membrane interaction energies for members of each subgroup of the family, and performed Molecular Dynamics simulations that have shown different configurations for the initial interaction between FABPs and membranes. In order to generalize our hypothesis, we extended the electrostatic and bioinformatics analysis over FABPs of different mammalian genus. Also, our methodological approach could be used for other systems involving protein–membrane interactions.
format Articulo
Articulo
author Zamarreño, Fernando
Giorgetti, Alejandro
Amundarain, María Julia
Viso, Juan Francisco
Córsico, Betina
Costabel, Marcelo Daniel
author_facet Zamarreño, Fernando
Giorgetti, Alejandro
Amundarain, María Julia
Viso, Juan Francisco
Córsico, Betina
Costabel, Marcelo Daniel
author_sort Zamarreño, Fernando
title Conserved charged amino acids are key determinants for fatty acid binding proteins (FABPs)-membrane interactions : A multi-methodological computational approach
title_short Conserved charged amino acids are key determinants for fatty acid binding proteins (FABPs)-membrane interactions : A multi-methodological computational approach
title_full Conserved charged amino acids are key determinants for fatty acid binding proteins (FABPs)-membrane interactions : A multi-methodological computational approach
title_fullStr Conserved charged amino acids are key determinants for fatty acid binding proteins (FABPs)-membrane interactions : A multi-methodological computational approach
title_full_unstemmed Conserved charged amino acids are key determinants for fatty acid binding proteins (FABPs)-membrane interactions : A multi-methodological computational approach
title_sort conserved charged amino acids are key determinants for fatty acid binding proteins (fabps)-membrane interactions : a multi-methodological computational approach
publishDate 2017
url http://sedici.unlp.edu.ar/handle/10915/148171
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bdutipo_str Repositorios
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