CIQUIBIC   05472
CENTRO DE INVESTIGACIONES EN QUIMICA BIOLOGICA DE CORDOBA
Unidad Ejecutora - UE
congresos y reuniones científicas
Título:
Protein-dependent Structuring of Myelin Monolayer
Autor/es:
ROSETTI C M, MAGGIO B
Lugar:
Montevideo, Uruguay
Reunión:
Congreso; . 6º conferencia internacional de Física Biológica. 5º Congreso de Biofísica del cono sur. 34º reunión anual de la Sociedad Argentina de Biofísica; 2007
Resumen:
The relationship between simple model mixtures and biological membranes, which contain hundreds of different proteins and lipids, is not clear. Some of the simple mixtures employed are not good mimics of cell membrane components. We intend to understand some rules for the distribution of components in a complex membrane. Monolayers of the natural Myelin membrane, that conserve all the compositional complexity of the natural membrane, are used as model system. Although the results cannot be directly extrapolate to the bilayer behavior, this system has the advantage of permitting the control of the surface properties (pressure, surface potential and pattern) as the composition is systematically changed. After the isolation of the lipid components and the major proteins (Myelin Basic Protein (MBP) and Folch Lees Proteolipid Protein (PLP)), we studied reconstituted mixtures of myelin lipids and one or both proteins. We determined the role of MBP and PLP on the structural dynamics of the interface.