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A11-positive β-amyloid Oligomer Preparation and Assessment Using Dot Blotting Analysis
Published on: May 22, 2018
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Environmental Control of Amyloid Polymorphism by Modulation of Hydrodynamic Stress
Jiangtao Zhou1, Leonardo Venturelli1, Ludovic Keiser2
1Laboratory of Physics of Living Matter, École Polytechnique Fédérale de Lausanne (EPFL), CH-1015 Lausanne, Switzerland.
ACS Nano
|December 22, 2020
Summary
Environmental stress influences amyloid structure. High stress yields uniform rod-like fibrils, while low stress produces diverse amyloid polymorphs, offering insights into disease and biomaterial design.
Area of Science:
- Biochemistry
- Materials Science
- Neuroscience
Background:
- Amyloid polymorphism is crucial for protein aggregation.
- Understanding amyloid origins is vital for neurodegenerative disease research and biomaterial development.
- Physicochemical factors controlling amyloid polymorphs are not well understood.
Purpose of the Study:
- To investigate the association between amyloid polymorphism and environmental stress.
- To explore the impact of air/water interface motion on amyloid fibril formation.
- To determine how different stress levels modulate amyloid polymorph diversity.
Main Methods:
- Inducing environmental stress in solution using a moving air/water interface.
- Characterizing amyloid polymorphs formed under varying stress conditions.
- Analyzing the conversion of fibril structures under high-stress environments.
Main Results:
- Low-stress environments resulted in heterogeneous amyloid polymorphs (twisted, helical, rod-like fibrils).
- High-stress conditions exclusively produced homogeneous rod-like fibrils.
- High environmental stress induced the conversion of twisted fibrils to rod-like fibrils, both during and after fibril maturation.
Conclusions:
- Environmental stress, particularly from a moving air/water interface, is a key factor in amyloid polymorphism.
- Controlled environmental stress can be used to fabricate homogeneous amyloid biomaterials.
- This research deepens the understanding of pathological amyloid polymorphism and its biotechnological implications.
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