INVESTIGADORES
NOLAN Maria Veronica
congresos y reuniones científicas
Título:
Interacción de Proteína Básica que une ácidos grasos con membranas lipídicas
Autor/es:
MARÍA VERÓNICA NOLAN, MASSIMILIANO PERDUCA, HUGO MÓNACO, BRUNO MAGGIO Y GUILLERMO MONTICH
Lugar:
Campinhas
Reunión:
Congreso; IV Congreso de Biofísica del Cono Sur,; 2000
Institución organizadora:
Sociedades argentina y brasilera de Biofísica
Resumen:
We have studied the interaction of ChL-FABP with POPC and
POPG. At low ionic strength, a filtration assay indicates that ChL-FABP
binds to POPG LUVs but not to POPC. According to the shift in the absorption
spectra of the single trp, ChL-FABP pure or in the presence of POPC unfolds at
60°C. Oppostite spectral shift are observed in the presence of POPG, probably
because the protein is already partly unfolded in the POPG membrane. When bound
to POPG at 25°C, FT-IR spectroscopy indicates a loss of b-structure; rthis
change occurs without changes in the Trp environment according to the
fluorescence emision spectra. In the presence of 0.1 M NaCl we have not
detected binding to POPC or to POPG LUVs. These results suggest that both
hidrophobic and electrostatic interactions are involved in the binding of
ChL-FABP to membranes.