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Reconstituted P2/myelin-lipid multilayers.

J Sedzik, A E Blaurock, M Hoechli

    Journal of Neurochemistry
    |September 1, 1985
    PubMed
    Summary
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    Bovine P2 protein interacts with myelin lipid vesicles, forming multilayers. X-ray diffraction reveals P2 protein resides in the interbilayer space, influencing myelin structure.

    Area of Science:

    • Biochemistry
    • Structural Biology
    • Neuroscience

    Background:

    • Myelin basic protein (MBP) is a major component of the myelin sheath.
    • The P2 protein is another significant myelin protein involved in nervous system structure.

    Purpose of the Study:

    • To investigate the structural complex formed between bovine P2 protein and myelin lipid vesicles.
    • To determine the location and structural impact of P2 protein within lipid bilayers.

    Main Methods:

    • Biochemical analysis
    • Freeze-fracture electron microscopy (FF EM)
    • Thin-section electron microscopy (EM)
    • X-ray diffraction

    Main Results:

    • P2 protein addition to lipid vesicles induced aggregation, fusion, and multilayer formation.

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  • X-ray diffraction showed a constant repeating distance of 86.0 ± 0.7 Å in multilayers with 4-15 wt% P2.
  • Electron density profiles indicated P2 protein is primarily located in the interbilayer spaces, with some insertion into lipid headgroups.

    • Conclusions:

    • Bovine P2 protein is a peripheral membrane protein that binds to myelin lipid bilayers.
    • The P2 protein occupies the interbilayer space, widening it compared to MBP, suggesting a globular structure.
    • Variations in P2 protein proportions across species may correlate with observed myelin structure differences.