Interaction of myelin basic protein isoforms with lipid bilayers studied by FTIR spectroscopy

Michael Jackson; Lin-P'ing Choo; Christopher Boulias; Mario A. Moscarello; Henry H. Mantsch

doi:10.1117/12.145247

1 May 1993 Interaction of myelin basic protein isoforms with lipid bilayers studied by FTIR spectroscopy

Michael Jackson, Lin-P'ing Choo, Christopher Boulias, Mario A. Moscarello, Henry H. Mantsch

Proceedings Volume 1890, Biomolecular Spectroscopy III; (1993) https://doi.org/10.1117/12.145247
Event: OE/LASE'93: Optics, Electro-Optics, and Laser Applications in Scienceand Engineering, 1993, Los Angeles, CA, United States

Abstract

The secondary structure of the naturally occurring isoforms of myelin basic protein (MBP1-8) from human myelin was studied by Fourier transform infrared spectroscopy under a variety of experimental conditions. In aqueous solution each isoform was found to be unstructured. In the presence of negatively charged liquid bilayers MBP1-4 were shown to exhibit an amide I band maximum indicative of the adoption of (alpha) -helical secondary structures. A detailed analysis revealed that significant proportions of (beta) -sheet secondary structure were also present. MBP5 and MBP8, which have significantly less cationic charge than MBP1-4, exhibited an amide I maximum identical to that seen in solution, suggesting that no interaction with the bilayer occurred. Analysis of the lipid CH₂ and C equals O stretching vibrations also pointed towards significant interaction of MBP1-4 with the bilayer. The changes in intensity and frequency of these bands which typically accompany the phase transition in the pure bilayer were abolished by addition of the proteins. No such effect was seen for MBP5 and 8, the normal lipid phase transition being apparent. The implications of these results in the aetiology of multiple sclerosis is discussed.

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Michael Jackson, Lin-P'ing Choo, Christopher Boulias, Mario A. Moscarello, and Henry H. Mantsch "Interaction of myelin basic protein isoforms with lipid bilayers studied by FTIR spectroscopy", Proc. SPIE 1890, Biomolecular Spectroscopy III, (1 May 1993); https://doi.org/10.1117/12.145247

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