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

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.