期刊
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
卷 -, 期 -, 页码 -出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.202215785
关键词
Amyloid; Annular Oligomers; Electron Microscopy; Protofibrils; Structure
The accumulation of amyloid-beta peptides (Aβ) is crucial in Alzheimer's disease development. The interaction between various Aβ assemblies and lipid membranes or membrane receptors result in increased membrane permeability and cellular homeostasis disruption, which plays a key role in the pathology of Alzheimer's disease. Aβ can affect lipid membranes in multiple ways, including a carpeting effect, a detergent effect, and the formation of Aβ ion-channel pores. Recent advancements in imaging techniques have improved our understanding of Aβ-induced membrane disruption. Understanding the relationship between different Aβ structures and membrane permeability will guide the development of therapeutics targeting Aβ cytotoxicity.
The accumulation of the amyloid-beta peptides (A beta) is central to the development of Alzheimer's disease. The mechanism by which A beta triggers a cascade of events that leads to dementia is a topic of intense investigation. A beta self-associates into a series of complex assemblies with different structural and biophysical properties. It is the interaction of these oligomeric, protofibril and fibrillar assemblies with lipid membranes, or with membrane receptors, that results in membrane permeability and loss of cellular homeostasis, a key event in Alzheimer's disease pathology. A beta can have an array of impacts on lipid membranes, reports have included: a carpeting effect; a detergent effect; and A beta ion-channel pore formation. Recent advances imaging these interactions are providing a clearer picture of A beta induced membrane disruption. Understanding the relationship between different A beta structures and membrane permeability will inform therapeutics targeting A beta cytotoxicity.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据