The self-organization of lipids and proteins of myelin at the membrane interface. Molecular factors undelying the microheterogeneity of domain segregation.

ROSETTI, C. M.; MAGGIO, B.; RAFAEL GUSTAVO OLIVEIRA

BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES

Elsevier

Año: 2008 vol. 1778 p. 1665 - 1665

0005-2736

he advances over the last 10 years on the understanding of myelin heterogeneity are reviewed. The main focus is on the applicability of Langmuir monolayers, Langmuir-Blodgett films and some associated techniques to unravelling the behaviour of interfaces formed with all the components of a natural membrane. Lipid-protein lateral segregation appears as a major driving force to determine surface patterns that can change under compression from circular domains to two-dimensional fractal structures. The major proteins of the myelin membrane induce lateral segregation in an otherwise homogeneous surface formed by the mixture of total myelin lipids. The lipid and protein components appear to distribute in the surface domains according to their charge, compressibility and relative molecular weight: myelin proteins, ganglioside GM1 and fluorescent lipid probes partition into liquid-expanded phase domains; other components such as phosphatidylserine and galactocerebroside partition into anothe