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.
Mintzer
Evan
E
Department of Chemistry and Biochemistry, Queens College of CUNY, Flushing, NY 11367-1597, USA.
Sargsyan
Hasmik
H
Bittman
Robert
R
D000595:Amino Acid Sequence; D018260:Gelsolin / Q000378:metabolism*; D008070:Lipopolysaccharides / Q000737:chemistry / Q000378:metabolism*; D008246:Lysophospholipids / Q000737:chemistry / Q000378:metabolism*; D008969:Molecular Sequence Data; D019269:Phosphatidylinositol 4,5-Diphosphate / Q000378:metabolism*; D011485:Protein Binding / Q000187:drug effects; D017434:Protein Structure, Tertiary; D013816:Thermodynamics
D018260:Gelsolin; D008070:Lipopolysaccharides; D008246:Lysophospholipids; D019269:Phosphatidylinositol 4,5-Diphosphate; C032881:lysophosphatidic acid