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髓鞘碱性蛋白掺入磷脂层的效果的微观结构分析。

Microstructural analysis of the effects of incorporation of myelin basic protein in phospholipid layers.

作者信息

Cristofolini L, Fontana M P, Serra F, Fasano A, Riccio P, Konovalov O

机构信息

Dipartmento di Fisica e Istituto Nazionale per la Fisica della Materia, Universita' di Parma, Parco Area delle Scienze 7a, 43100 Parma, Italy.

出版信息

Eur Biophys J. 2005 Nov;34(8):1041-8. doi: 10.1007/s00249-005-0489-5. Epub 2005 May 26.

Abstract

We report an X-ray reflectivity study on the effects of adsorption of myelin basic protein (MBP) on Langmuir monolayers and on deposited Langmuir-Schaefer multilayers of the phospholipid dipalmitoyl phosphatidylglycerol (DPPG). We provide for the first time, direct microscopic evidence on the destructuring effects of MBP leading to plasticity of the DPPG layers supporting commonly accepted models of the stabilizing role of MBP in the myelin membrane. We also show how protein adsorption onto the layer is determined both by electrostatic and nonspecific hydrophobic interactions.

摘要

我们报告了一项关于髓鞘碱性蛋白(MBP)吸附对磷脂二棕榈酰磷脂酰甘油(DPPG)的朗缪尔单层膜和沉积的朗缪尔-谢弗多层膜影响的X射线反射率研究。我们首次提供了直接的微观证据,证明MBP的解构作用导致DPPG层的可塑性,这支持了MBP在髓鞘膜中起稳定作用的普遍接受的模型。我们还展示了蛋白质在层上的吸附是如何由静电和非特异性疏水相互作用共同决定的。

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