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Protein-induced surface structuring in myelin membrane monolayers.

Carla M Rosetti¹, Bruno Maggio

¹Centro de Investigaciones en Química Biológica de Córdoba, Departamento de Química Biológica, Facultad de Ciencias Químicas, Universidad Nacional de Córdoba, Ciudad Universitaria, Córdoba, Argentina.

Biophysical Journal

|October 2, 2007

Summary

Myelin basic protein (MBP) and proteolipid protein (PLP) influence myelin membrane structure at the air-water interface differently. MBP stabilizes liquid phases, while PLP forms fractal patterns, revealing distinct roles in membrane dynamics.

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Area of Science:

Biophysics
Membrane Biophysics
Materials Science

Background:

Myelin membranes exhibit complex compositional integrity when forming monolayers at the air-water interface.
These monolayers display intricate pressure-dependent surface patterns, transitioning from liquid phase coexistence to a viscous fractal phase upon compression.

Purpose of the Study:

To elucidate the specific roles of myelin basic protein (MBP) and Folch-Lees proteolipid protein (PLP) in governing the structural dynamics of myelin monolayers.
To understand how individual protein components influence the behavior of myelin lipids at the air-water interface.

Main Methods:

Preparation of myelin monolayers at the air-water interface.
Analysis of surface pressure-dependent behavior of mixed monolayers containing myelin lipids and either MBP or PLP.
Characterization of surface topography and structural dynamics.

Main Results:

MBP and PLP exhibit distinct pressure-dependent behaviors in myelin monolayers.
MBP stabilizes liquid phase segregation at low pressures and is extruded upon compression.
PLP induces fractal-like patterns across all surface pressures and acts as a structural scaffold, while MBP mediates pressure-dependent extrusion and adsorption.

Conclusions:

The structural organization and dynamics of myelin monolayers are governed by the interplay of near-equilibrium and out-of-equilibrium effects.
MBP and PLP play differential, crucial roles in regulating myelin membrane structure and behavior at interfaces.