Fatty acid transfer from intestinal fatty acid binding protein to membranes: Electrostatic and hydrophobic interactions

Intestinal fatty acid binding protein (IFABP) is thought to participate in the intracellular transport of fatty acids (FAs). Fatty acid transfer from IFABP to phospholipid membranes is proposed to occur during protein-membrane collisional interactions. In this study, we analyzed the participation of...

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Detalles Bibliográficos
Autores principales: Córsico, Betina, Franchini, Gisela Raquel, Hsu, Kuo Tung, Storch, Judith
Formato: Articulo
Lenguaje:Inglés
Publicado: 2005
Materias:
Ciencias Médicas
Chemical modification of proteins
Fatty acid transfer mechanism
Intracellular lipid-binding proteins
Protein acetylation
Structure-function analysis
Acceso en línea:http://sedici.unlp.edu.ar/handle/10915/83020
Aporte de:
SEDICI (UNLP) de Universidad Nacional de La Plata
id I19-R120-10915-83020
record_format dspace
institution Universidad Nacional de La Plata
institution_str I-19
repository_str R-120
collection SEDICI (UNLP)
language Inglés
topic Ciencias Médicas
Chemical modification of proteins
Fatty acid transfer mechanism
Intracellular lipid-binding proteins
Protein acetylation
Structure-function analysis
spellingShingle Ciencias Médicas
Chemical modification of proteins
Fatty acid transfer mechanism
Intracellular lipid-binding proteins
Protein acetylation
Structure-function analysis
Córsico, Betina
Franchini, Gisela Raquel
Hsu, Kuo Tung
Storch, Judith
Fatty acid transfer from intestinal fatty acid binding protein to membranes: Electrostatic and hydrophobic interactions
topic_facet Ciencias Médicas
Chemical modification of proteins
Fatty acid transfer mechanism
Intracellular lipid-binding proteins
Protein acetylation
Structure-function analysis
description Intestinal fatty acid binding protein (IFABP) is thought to participate in the intracellular transport of fatty acids (FAs). Fatty acid transfer from IFABP to phospholipid membranes is proposed to occur during protein-membrane collisional interactions. In this study, we analyzed the participation of electrostatic and hydrophobic interactions in the collisional mechanism of FA transfer from IFABP to membranes. Using a fluorescence resonance energy transfer assay, we examined the rate and mechanism of transfer of anthroyloxy-fatty acid analogs a) from IFABP to phospholipid membranes of different composition; b) from chemically modified IFABPs, in which the acetylation of surface lysine residues eliminated positive surface charges; and c) as a function of ionic strength. The results show clearly that negative charges on the membrane surface and positive charges on the protein surface are important for establishing the "collisional complex," during which fatty acid transfer occurs. In addition, changes in the hydrophobicity of the protein surface, as well as the hydrophobic volume of the acceptor vesicles, also influenced the rate of fatty acid transfer. Thus, ionic interactions between IFABP and membranes appear to play a primary role in the process of fatty acid transfer to membranes, and hydrophobic interactions can also modulate the rates of ligand transfer.
format Articulo
Articulo
author Córsico, Betina
Franchini, Gisela Raquel
Hsu, Kuo Tung
Storch, Judith
author_facet Córsico, Betina
Franchini, Gisela Raquel
Hsu, Kuo Tung
Storch, Judith
author_sort Córsico, Betina
title Fatty acid transfer from intestinal fatty acid binding protein to membranes: Electrostatic and hydrophobic interactions
title_short Fatty acid transfer from intestinal fatty acid binding protein to membranes: Electrostatic and hydrophobic interactions
title_full Fatty acid transfer from intestinal fatty acid binding protein to membranes: Electrostatic and hydrophobic interactions
title_fullStr Fatty acid transfer from intestinal fatty acid binding protein to membranes: Electrostatic and hydrophobic interactions
title_full_unstemmed Fatty acid transfer from intestinal fatty acid binding protein to membranes: Electrostatic and hydrophobic interactions
title_sort fatty acid transfer from intestinal fatty acid binding protein to membranes: electrostatic and hydrophobic interactions
publishDate 2005
url http://sedici.unlp.edu.ar/handle/10915/83020
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AT franchinigiselaraquel fattyacidtransferfromintestinalfattyacidbindingproteintomembraneselectrostaticandhydrophobicinteractions
AT hsukuotung fattyacidtransferfromintestinalfattyacidbindingproteintomembraneselectrostaticandhydrophobicinteractions
AT storchjudith fattyacidtransferfromintestinalfattyacidbindingproteintomembraneselectrostaticandhydrophobicinteractions
bdutipo_str Repositorios
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