近期关于阿尔茨海默病中淀粉样β和tau 与膜相互作用的计算进展。
Recent Computational Advances Regarding Amyloid-β and Tau Membrane Interactions in Alzheimer's Disease.
机构信息
CNRS, Laboratoire de Biochimie Théorique, Institut de Biologie Physico-Chimique, Fondation Edmond de Rothschild, Université Paris Cité, UPR 9080, 13 rue Pierre et Marie Curie, 75005 Paris, France.
Institut Universitaire de France (IUF), 75005 Paris, France.
出版信息
Molecules. 2023 Oct 13;28(20):7080. doi: 10.3390/molecules28207080.
The interactions of amyloid proteins with membranes have been subject to many experimental and computational studies, as these interactions contribute in part to neurodegenerative diseases. In this review, we report on recent simulations that have focused on the adsorption and insertion modes of amyloid-β and tau proteins in membranes. The atomistic-resolution characterization of the conformational changes of these amyloid proteins upon lipid cell membrane and free lipid interactions is of interest to rationally design drugs targeting transient oligomers in Alzheimer's disease.
淀粉样蛋白与膜的相互作用一直是许多实验和计算研究的主题，因为这些相互作用是导致神经退行性疾病的部分原因。在这篇综述中，我们报告了最近的一些模拟研究，这些研究集中在淀粉样-β和 tau 蛋白在膜中的吸附和插入模式上。这些淀粉样蛋白在与细胞膜脂质和游离脂质相互作用时构象变化的原子分辨率表征，对于合理设计针对阿尔茨海默病中瞬态低聚物的药物具有重要意义。
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