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Structural Dynamics of Myelin Basic Protein in the Assembly of a Model Membrane

  • P. Cavatorta
  • L. Masotti
  • A. G. Szabo
  • P. Riccio
  • E. Quagliariello
Conference paper

Abstract

The encephalitogenic myelin basic protein (MBP), with a MW of 18.4 KDa protein, is the smallest of the CNS myelin proteins, and accounts for about 30% of their total content (Boggs et al., 1982). MBP, when extracted with organic solvents, is soluble in water and has been extensively studied because of its ability to induce inflammatory demyelination (Kies et al., 1965). Recently Riccio et al. (1986) reported EM evidence that MBP, extracted with endogenous lipids employing the detergent CTAB, was able to induce lysolecithin to undergo a structural transition from micelles into multilamellar vesicles. On the other hand lipid-free MBP interacted with lysolecithin but was not able to induce such a transition. The aim of this work is to study the ability of lipids to modulate protein conformation and of a protein such as MBP to influence lipid supramolecular organization. Static and time resolved fluorescence of the single tryptophan residue of MBP and CD measurements are presented that illustrate interesting details of the molecular dynamics involved in lipid protein interactions.

Keywords

Quantum Yield Myelin Basic Protein Quench Rate Constant Multilamellar Vesicle Endogenous Lipid 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

  1. Boggs, J. M., Moscarello, M. A., and Papahadjopoulos, D., 1982, in: Lipid-Protein Interaction, Vol. 2, P. C. Jost and O. H. Griffith, eds., page 1–51, John Wiley, New York.Google Scholar
  2. Deibler, G. E., Martenson, R. E., and Kies, M. W., 1972, Prep. Biochem., 2:139.PubMedCrossRefGoogle Scholar
  3. Kies, M. W., Alvord, E. C., Mortenson, R. E., and LeBaron, F. N., 1965, Science, 151:821.CrossRefGoogle Scholar
  4. Masotti, L., Cavatorta, P., Szabo, A. G., Farruggia, G., Sartor, G., this volume.Google Scholar
  5. Riccio, P., Masotti, L., Cavatorta, P., DeSantis, A., Juretic, D., Bobba, A., Pasquali-Ronchetti, I., and Quagliariello, E., 1986, Biochem. Biophys. Res. Comm., 134:313.PubMedCrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1989

Authors and Affiliations

  • P. Cavatorta
    • 1
  • L. Masotti
    • 2
  • A. G. Szabo
    • 3
  • P. Riccio
    • 4
  • E. Quagliariello
    • 4
  1. 1.Dept. of Biphysics-GNCBUniversity of ParmaParmaItaly
  2. 2.Institute of Biological ChemistryUniversity of ParmaParmaItaly
  3. 3.Division of Biological SciencesNational Research Council of CanadaOttawaCanada
  4. 4.Inst. of Biological ChemistryUniversity of BariBariItaly

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