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Reconstituted P2/myelin-lipid multilayers
Journal of Neurochemistry
|September 1, 1985
Summary
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.
- 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.