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用μ子自旋旋转研究人脑铁蛋白:一项初步研究。

Human-brain ferritin studied by muon spin rotation: a pilot study.

作者信息

Bossoni Lucia, Grand Moursel Laure, Bulk Marjolein, Simon Brecht G, Webb Andrew, van der Weerd Louise, Huber Martina, Carretta Pietro, Lascialfari Alessandro, Oosterkamp Tjerk H

机构信息

Huygens-Kamerlingh Onnes Laboratory, Leiden University, 2333 CA Leiden, Netherlands.

出版信息

J Phys Condens Matter. 2017 Oct 18;29(41):415801. doi: 10.1088/1361-648X/aa80b3. Epub 2017 Sep 5.

Abstract

Muon spin rotation is employed to investigate the spin dynamics of ferritin proteins isolated from the brain of an Alzheimer's disease (AD) patient and of a healthy control, using a sample of horse-spleen ferritin as a reference. A model based on the Néel theory of superparamagnetism is developed in order to interpret the spin relaxation rate of the muons stopped by the core of the protein. Using this model, our preliminary observations show that ferritins from the healthy control are filled with a mineral compatible with ferrihydrite, while ferritins from the AD patient contain a crystalline phase with a larger magnetocrystalline anisotropy, possibly compatible with magnetite or maghemite.

摘要

利用μ子自旋旋转技术,以马脾铁蛋白样本作为参考,研究从阿尔茨海默病(AD)患者大脑和健康对照者大脑中分离出的铁蛋白蛋白质的自旋动力学。为了解释被蛋白质核心捕获的μ子的自旋弛豫率,建立了一个基于超顺磁性奈尔理论的模型。利用该模型,我们的初步观察结果表明,来自健康对照者的铁蛋白填充有一种与水铁矿相容的矿物质,而来自AD患者的铁蛋白含有一种具有较大磁晶各向异性的晶相,可能与磁铁矿或磁赤铁矿相容。

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