Knoll Wiebke, Peters Judith, Kursula Petri, Gerelli Yuri, Ollivier Jacques, Demé Bruno, Telling Mark, Kemner Ewout, Natali Francesca
University Joseph Fourier UFR PhITEM, Grenoble, France.
Soft Matter. 2014 Jan 21;10(3):519-29. doi: 10.1039/c3sm51393a.
The myelin sheath is a tightly packed, multilayered membrane structure wrapped around selected nerve axons in the central and the peripheral nervous system. Because of its electrical insulation of the axons, which allows fast, saltatory nerve impulse conduction, myelin is crucial for the proper functioning of the vertebrate nervous system. A subset of myelin-specific proteins is well-defined, but their influence on membrane dynamics, i.e. myelin stability, has not yet been explored in detail. We investigated the structure and the dynamics of reconstituted myelin membranes on a pico- to nanosecond timescale, influenced by myelin basic protein (MBP) and myelin protein 2 (P2), using neutron diffraction and quasi-elastic neutron scattering. A model for the scattering function describing molecular lipid motions is suggested. Although dynamical properties are not affected significantly by MBP and P2 proteins, they act in a highly synergistic manner influencing the membrane structure.
髓鞘是一种紧密堆积的多层膜结构，包裹着中枢神经系统和周围神经系统中选定的神经轴突。由于其对轴突的电绝缘作用，使得神经冲动能够快速跳跃式传导，髓鞘对于脊椎动物神经系统的正常运作至关重要。一部分髓鞘特异性蛋白已被明确界定，但其对膜动力学（即髓鞘稳定性）的影响尚未得到详细研究。我们利用中子衍射和准弹性中子散射，在皮秒到纳秒的时间尺度上研究了受髓鞘碱性蛋白（MBP）和髓鞘蛋白2（P2）影响的重组髓鞘膜的结构和动力学。提出了一个描述分子脂质运动的散射函数模型。尽管动力学性质不受MBP和P2蛋白的显著影响，但它们以高度协同的方式作用，影响膜结构。
