Interaction of Chicken Liver Basic Fatty Acid-Binding Protein with Lipid Membranes

VERÓNICA NOLAN, MASSIMILIANO PERDUCA, HUGO MÓNACO, BRUNO MAGGIO AND GUILLERMO MONTICH

BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES

Elsevier

Año: 2003 vol. 1611 p. 98 - 106

0005-2736

  The interaction of chicken liver basic fatty acid-binding protein (Lb-FABP) with large unilamelar vesicles (LUVs) of palmitoyloleoyl phosphatidylcholine (POPC) and palmitoyloleoyl phosphatidylglycerol (POPG) were studied by binding assays, Fourier transform infrarred (FT-IR) spectroscopy, monolayers at air-water interfaces, and low-angle X-ray diffraction. Lb-FABP binds to POPG LUVs at low ionic strength but not at 0.1 M NaCl. Thew infrared (IR) spectra of the POPG membrane-bound protein showed a decrease of the band corresponding to b-structures as compared to the protein in solution. In addition, a cooperative decrease of the b-edge band above 70°C in solution was also evident, while the transiton was less cooperative and took place at lower temperature for the POPG membrane-bound protein. Low- and wide-angle X-ray diffraction experiments with lipid multilayers indicate that binding of the protein produces a rearrengment of the membrane structure, increasing the interlamellar spacing and decreasing the compactness of the lipids.