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首页> 外文会议>Biomolecular Spectroscopy III >Interaction of myelin basic protein isoforms with lipid bilayers studied by FTIR spectroscopy
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Interaction of myelin basic protein isoforms with lipid bilayers studied by FTIR spectroscopy

机译：FTIR光谱研究髓磷脂碱性蛋白同工型与脂质双层的相互作用

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摘要

Abstract: ondary 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 $beta@-sheet secondary structure were also present. MBP5 and MBP8, which have significantly less cationic charge than MBP1-4, exhibited an amide I maximum identical to that seen in solution, suggesting that no interaction with the bilayer occurred. Analysis of the lipid CH$-2$/ and C $EQ O stretching vibrations also pointed towards significant interaction of MBP1-4 with the bilayer. The changes in intensity and frequency of these bands which typically accompany the phase transition in the pure bilayer were abolished by addition of the proteins. No such effect was seen for MBP5 and 8, the normal lipid phase transition being apparent. The implications of these results in the aetiology of multiple sclerosis is discussed.!0
机译：摘要：在多种实验条件下，通过傅立叶变换红外光谱法研究了人髓磷脂中髓鞘碱性蛋白（MBP1-8）天然同工型的二元结构。发现在水溶液中每种同工型都是无结构的。在带负电荷的液体双层中，MBP1-4显示出最大的酰胺I带，表明采用了α-螺旋二级结构。详细的分析表明，也存在大量的$ beta @ -sheet二级结构。 MBP5和MBP8的阳离子电荷比MBP1-4少得多，其酰胺I最大与溶液中看到的相同，表明没有发生与双层的相互作用。对脂质CH $ -2 $ /和C $ EQ O的拉伸振动的分析也指出MBP1-4与双层的显着相互作用。通过添加蛋白质消除了纯双分子层中通常伴随相变的这些条带的强度和频率变化。对于MBP5和8没有看到这种作用，正常的脂质相变是明显的。讨论了这些结果在多发性硬化病的病因中的意义!! 0

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