INIBIOLP   05426
INSTITUTO DE INVESTIGACIONES BIOQUIMICAS DE LA PLATA "PROF. DR. RODOLFO R. BRENNER"
Unidad Ejecutora - UE
artículos
Título:
Lipid packing determines proteinmembrane interactions: Challenges for
Autor/es:
SANCHEZ, S. A.; TRICERRI, M. A.; OSSATO, G.; GRATTON, E.
Revista:
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
Editorial:
ELSEVIER SCIENCE BV
Referencias:
Año: 2010 vol. 1789 p. 1399 - 1408
ISSN:
0005-2736
Resumen:
Protein and proteinlipid interactions, with and within specific areas in the cell membrane, are critical in
order to modulate the cell signaling events required to maintain cell functions and viability. Biological
bilayers are complex, dynamic platforms, and thus in vivo observations usually need to be preceded by
studies on model systems that simplify and discriminate the different factors involved in lipidprotein
interactions. Fluorescence microscopy studies using giant unilamellar vesicles (GUVs) as membrane model
systems provide a unique methodology to quantify protein binding, interaction, and lipid solubilization in
artificial bilayers. The large size of lipid domains obtainable on GUVs, together with fluorescence microscopy
techniques, provides the possibility to localize and quantify molecular interactions. Fluorescence Correlation
Spectroscopy (FCS) can be performed using the GUV model to extract information on mobility and
concentration. Two-photon Laurdan Generalized Polarization (GP) reports on local changes in membrane
water content (related to membrane fluidity) due to protein binding or lipid removal from a given lipid
domain. In this review, we summarize the experimental microscopy methods used to study the interaction of
human apolipoprotein A-I (apoA-I) in lipid-free and lipid-bound conformations with bilayers and natural
membranes. Results described here help us to understand cholesterol homeostasis and offer a
methodological design suited to different biological systems