Lysophosphatidic acid and lipopolysaccharide bind to the PIP2-binding domain of gelsolin

Biochim Biophys Acta. 2006 Jan;1758(1):85-9. doi: 10.1016/j.bbamem.2005.12.009. Epub 2006 Jan 18.


The binding of the gelsolin P2 peptide (residues 150-169) with lysophosphatidic acid (LPA) and lipopolysaccharide (LPS) was investigated by isothermal titration calorimetry. P2 binds to LPS with higher affinity than to LPA. For the interaction of 1-oleoyl-LPA with P2 in the absence of salt, K(d) and deltaH degrees were 920 nM and -2.07 kcal/mol, respectively, at pH 7.4 and 25 degrees C. For the interaction of lipopolysaccharide (LPS) from P. aeruginosa with P2 under the same conditions, K(d) was 177 nM and deltaH degrees was -7.6 kcal/mol.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Amino Acid Sequence
  • Gelsolin / metabolism*
  • Lipopolysaccharides / chemistry
  • Lipopolysaccharides / metabolism*
  • Lysophospholipids / chemistry
  • Lysophospholipids / metabolism*
  • Molecular Sequence Data
  • Phosphatidylinositol 4,5-Diphosphate / metabolism*
  • Protein Binding / drug effects
  • Protein Structure, Tertiary*
  • Thermodynamics


  • Gelsolin
  • Lipopolysaccharides
  • Lysophospholipids
  • Phosphatidylinositol 4,5-Diphosphate
  • lysophosphatidic acid