Molecular and Cellular Biochemistry

, Volume 239, Issue 1, pp 45–54

Insights into binding of fatty acids by fatty acid binding proteins

  • Thorsten Hanhoff
  • Christian Lücke
  • Friedrich Spener

DOI: 10.1023/A:1020502624234

Cite this article as:
Hanhoff, T., Lücke, C. & Spener, F. Mol Cell Biochem (2002) 239: 45. doi:10.1023/A:1020502624234


Members of the phylogenetically related intracellular lipid binding protein (iLBP) are characterized by a highly conserved tertiary structure, but reveal distinct binding preferences with regard to ligand structure and conformation, when binding is assessed by the Lipidex method (removal of unbound ligand by hydrophobic polymer) or by isothermal titration calorimetry, a true equilibrium method. Subfamily proteins bind retinoids, subfamily II proteins bind bulky ligands, examples are intestinal bile acid binding protein (I-BABP) and liver fatty acid binding protein (L-FABP) which binds 2 ligand molecules, preferably monounsaturated and n-3 fatty acids. Subfamily III intestinal fatty acid binding protein (I-FABP) binds fatty acid in a bent conformation. The fatty acid bound by subfamily IV FABPs has a U-shaped conformation; here heart (H-) FABP preferably binds n-6, brain (B-) FABP n-3 fatty acids. The ADIFAB-method is a fluorescent test for fatty acid in equilibrium with iLBP and reveals some correlation of binding affinity to fatty acid solubility in the aqueous phase; these data are often at variance with those obtained by the other methods. Thus, in this review published binding data are critically discussed, taking into account on the one hand binding increments calculated for fatty acid double bonds on the basis of the ‘solubility’ hypothesis, on the other hand the interpretation of calorimetric data on the basis of crystallographic and solution structures of iLBPs.

FABP tertiary structure fatty acid binding ADIFAB isothermal titration calorimetry Lipidex 

Copyright information

© Kluwer Academic Publishers 2002

Authors and Affiliations

  • Thorsten Hanhoff
    • 1
  • Christian Lücke
    • 2
  • Friedrich Spener
    • 3
  1. 1.Department of BiochemistryUniversity of MünsterMünsterGermany
  2. 2.Institute of Biophysical ChemistryUniversity of FrankfurtFrankfurtGermany
  3. 3.Department of BiochemistryUniversity of MünsterMünsterGermany

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