期刊
BIOCHEMISTRY
卷 52, 期 5, 页码 808-817出版社
AMER CHEMICAL SOC
DOI: 10.1021/bi301070v
关键词
-
资金
- Brodie Discovery and Innovation Fund
- National Science Foundation [1054211]
- Alzheimer's Association [NIRG-11-203834]
- Div Of Civil, Mechanical, & Manufact Inn
- Directorate For Engineering [1054211] Funding Source: National Science Foundation
A diverse number of diseases, including Alzheimer's disease, Huntington's disease, and type 2 diabetes, are characterized by the formation of fibrillar protein aggregates termed amyloids. The precise mechanism by which aggregates are toxic remains unclear; however, these proteins have been shown to interact strongly with lipid membranes. We investigated morphological and mechanical changes in model lipid bilayers exposed to amyloid-forming proteins by reconstructing the tapping forces associated with atomic force microscopy (AFM) imaging in solution. Tip/sample tapping forces contain information regarding mechanical properties of surfaces. Interpretation of the mechanical changes in the bilayers was aided by numerical simulations of the entire AFM experiment. Amyloid-forming proteins disrupted distinct regions of the bilayer morphology, and these regions were associated with decreased Young's modulus and adhesive properties. These changes in bilayer mechanical properties upon exposure to amyloid-forming proteins may represent a common mechanism leading to membrane dysfunction in amyloid diseases.
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