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Proceedings Paper

Interaction of myelin basic protein isoforms with lipid bilayers studied by FTIR spectroscopy
Author(s): Michael Jackson; Lin-P'ing Choo; Christopher Boulias; Mario A. Moscarello; Henry H. Mantsch
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Paper 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.

Paper Details

Date Published: 1 May 1993
PDF: 4 pages
Proc. SPIE 1890, Biomolecular Spectroscopy III, (1 May 1993); doi: 10.1117/12.145247
Show Author Affiliations
Michael Jackson, National Research Council Canada (Canada)
Lin-P'ing Choo, National Research Council Canada (United States)
Christopher Boulias, Hospital for Sick Children (Canada)
Mario A. Moscarello, Hospital for Sick Children (Canada)
Henry H. Mantsch, National Research Council Canada (Canada)

Published in SPIE Proceedings Vol. 1890:
Biomolecular Spectroscopy III
Laurence A. Nafie; Henry H. Mantsch, Editor(s)

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