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Surface behavior of myelin monolayers

R G Oliveira1, R O Calderón, B Maggio

  • 1Departamento de Química Biológica-CIQUIBIC, Facultad de Ciencias Químicas, Universidad Nacional de Córdoba, Ag. Postal 4, CC 61, 5000 Córdoba, Argentina.

Biochimica Et Biophysica Acta
|May 2, 1998
PubMed
Summary

Myelin can form a stable monomolecular layer at the air-water interface. Its proteins undergo pressure-dependent organization changes, impacting the layer's stability and molecular packing.

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Area of Science:

  • Biophysics
  • Materials Science
  • Neuroscience

Background:

  • Myelin is a crucial lipid-rich membrane insulating nerve cells.
  • Understanding myelin's interfacial behavior is key to its function.

Purpose of the Study:

  • To investigate the biophysical properties of myelin monolayers at the air-water interface.
  • To determine how myelin's molecular components organize under surface pressure.

Main Methods:

  • Spreading myelin as a stable monomolecular layer at the air-water interface.
  • Measuring surface pressure-molecular area isotherms and surface potential.
  • Analyzing compressibility and hysteresis during compression-decompression cycles.

Main Results:

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  • Myelin monolayers exhibit reproducible properties with a collapse point at approximately 46 mN/m.
  • A significant change in compressibility and surface potential occurs around 20 mN/m.
  • Hysteresis in the first cycle suggests pressure-induced protein relocation without unfolding.

    • Conclusions:

    • Myelin's protein components reorganize under lateral surface pressure above 20 mN/m.
    • This reorganization significantly affects the monolayer's stability, packing, and dipolar organization.
    • The findings provide insights into myelin's interfacial behavior and structural dynamics.