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淀粉样β聚集体与磷脂膜的相互作用及其对神经退行性变的影响。

The interactions of amyloid β aggregates with phospholipid membranes and the implications for neurodegeneration.

作者信息

Budvytyte Rima, Valincius Gintaras

机构信息

Vilnius University, Life Sciences Center, Institute of Biochemistry, Sauletekio av. 7, Vilnius LT-10257, Lithuania.

出版信息

Biochem Soc Trans. 2023 Feb 27;51(1):147-159. doi: 10.1042/BST20220434.

DOI:10.1042/BST20220434
PMID:36629697
Abstract

Misfolding, aggregation and accumulation of Amyloid-β peptides (Aβ) in neuronal tissue and extracellular matrix are hallmark features of Alzheimer's disease (AD) pathology. Soluble Aβ oligomers are involved in neuronal toxicity by interacting with the lipid membrane, compromising its integrity, and affecting the function of receptors. These facts indicate that the interaction between Aβ oligomers and cell membranes may be one of the central molecular level factors responsible for the onset of neurodegeneration. The present review provides a structural understanding of Aβ neurotoxicity via membrane interactions and contributes to understanding early events in Alzheimer's disease.

摘要

淀粉样β肽(Aβ)在神经元组织和细胞外基质中的错误折叠、聚集和积累是阿尔茨海默病(AD)病理学的标志性特征。可溶性Aβ寡聚体通过与脂质膜相互作用、损害其完整性并影响受体功能而参与神经元毒性。这些事实表明,Aβ寡聚体与细胞膜之间的相互作用可能是导致神经退行性变发生的核心分子水平因素之一。本综述通过膜相互作用提供了对Aβ神经毒性的结构理解,并有助于理解阿尔茨海默病的早期事件。

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