The alpha-helical domain of liver fatty acid binding protein is responsible for the diffusion-mediated transfer of fatty acids to phospholipid membranes.

@article{Crsico2004TheAD,
  title={The alpha-helical domain of liver fatty acid binding protein is responsible for the diffusion-mediated transfer of fatty acids to phospholipid membranes.},
  author={Betina C{\'o}rsico and Heng-Ling Liou and Judith Storch},
  journal={Biochemistry},
  year={2004},
  volume={43 12},
  pages={
          3600-7
        }
}
Intestinal fatty acid binding protein (IFABP) and liver FABP (LFABP), homologous proteins expressed at high levels in intestinal absorptive cells, employ markedly different mechanisms for the transfer of fatty acids (FAs) to acceptor membranes. Transfer from IFABP occurs during protein-membrane collisional interactions, while for LFABP, transfer occurs by diffusion through the aqueous phase. Earlier, we had shown that the helical domain of IFABP is critical in determining its collisional FA… 
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The integrity of the alpha-helical domain of intestinal fatty acid binding protein is essential for the collision-mediated transfer of fatty acids to phospholipid membranes.
Protein-Membrane Interaction and Fatty Acid Transfer from Intestinal Fatty Acid-binding Protein to Membranes
TLDR
The hypothesis that the portal region undergoes a conformational change during protein-membrane interaction, which leads to release of the bound fatty acid to the membrane, is supported and that the α2 segment is of particular importance in the establishment of charge-charge interactions between IFABP and membranes.
Fatty acid transfer from intestinal fatty acid binding protein to membranes: electrostatic and hydrophobic interactions Published, JLR Papers in Press, May 1, 2005. DOI 10.1194/jlr.M500140-JLR200
TLDR
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.
Modeling fatty acid delivery from intestinal fatty acid binding protein to a membrane
TLDR
Although the domains can widen enough to allow the passage of palmitate, fatty acid release through the helical portal region incurs smaller conformational changes and a lower energetic cost.
Probing the Interaction of Brain Fatty Acid Binding Protein (B-FABP) with Model Membranes
TLDR
Brain fatty acid-binding protein (B-FABP) interacts with biological membranes and delivers polyunsaturated fatty acids (FAs) via a collisional mechanism through a motif called portal region, which leads to structural changes in the protein and in the membrane model induced by their interaction.
Intracellular lipid transport: structure–function relationships in fatty acid binding proteins
TLDR
It has been demonstrated that the α-helical region of FABP is involved in membrane interactions and appears to play a primary role, thus determining the mechanism of transfer of FA from FABPs to membranes.
Insight into the interaction sites between fatty acid binding proteins and their ligands
TLDR
It is suggested that the protein surface is capable of sequestering free fatty acids from solution, where brief encounters evolve into adsorbed states, which later mature by migration of the ligand into a more specific binding site.
Characterization of fatty acid binding and transfer from Δ98Δ, a functional all-β abridged form of IFABP.
Natural ligand binding and transfer from liver fatty acid binding protein (LFABP) to membranes.
Tryptophan Insertion Mutagenesis of Liver Fatty Acid-binding Protein
TLDR
The ability of bound oleoyl CoA to reduce the fluorescence of L28W provided an opportunity to demonstrate that fatty acyl CoAs can compete with fatty acids for binding to liver FABP under physiological conditions, further highlighting the role of fatty acYL CoAs in modulating FABp function in the cell.
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References

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TLDR
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TLDR
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TLDR
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TLDR
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TLDR
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