J. Lipid Res.
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A more recent version of this article appeared on August 1, 2005

Papers In Press, published online ahead of print May 1, 2005
J. Lipid Res., doi:10.1194/jlr.M500140-JLR200
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Submitted on April 11, 2005
Accepted on April 25, 2005

Electrostatic and hydrophobic interactions contribute to the collisional mechanism of fatty acid transfer from intestinal fatty acid binding protein to phospholipid membranes

Betina Córsico, Gisela R. Franchini, Kuo-Tung Hsu, and Judith Storch

Department of Nutritional Sciences, Rutgers University, New Brunswick, NJ 08901

Corresponding Author: storch{at}aesop.rutgers.edu

Intestinal fatty acid binding protein (IFABP) is thought to participate in intracellular transport of fatty acids (FA). 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 analogues (AOFA) a) from IFABP to phospholipid membranes of different composition; b) from chemically modified IFABP, where 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.


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L. J. Falomir-Lockhart, L. Laborde, P. C. Kahn, J. Storch, and B. Corsico
Protein-Membrane Interaction and Fatty Acid Transfer from Intestinal Fatty Acid-binding Protein to Membranes: SUPPORT FOR A MULTISTEP PROCESS
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