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

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DOIResolve DOI: http://doi.org/10.1117/12.145247
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TypeBook Chapter
Proceedings titleBiomolecular Spectroscopy III
Series titleSPIE Proceedings
ConferenceBiomolecular Spectroscopy III, January 17, 1993, Los Angeles, California, USA
ISSN0277-786X
Volume1890
Pages912; # of pages: 4
AbstractThe 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.
Publication date
PublisherSPIE
AffiliationNational Research Council Canada; NRC Institute for Biodiagnostics
Peer reviewedYes
NRC number320
NPARC number9742027
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Record identifierb4db3b75-df19-4816-b1a6-bd7f5fa5c4cb
Record created2009-07-17
Record modified2016-12-13
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