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Updated: Jun 11, 2026
15:04
Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils
Published on: September 28, 2019
Amyloidogenic protein-membrane interactions: mechanistic insight from model systems
Sara M Butterfield1, Hilal A Lashuel
1Laboratory of Molecular Neurobiology and Neuroproteomics, Swiss Federal Institute of Technology Lausanne (EPFL), SV-BMI-LMNN AI2351, 1015 Lausanne, Switzerland.
Angewandte Chemie (International Ed. in English)
|July 13, 2010
Summary
Amyloid-forming proteins harm cells by interacting with membranes, causing structural damage and toxicity. Their membrane-disrupting mechanisms resemble those of toxins.
Area of Science:
- Biochemistry
- Cell Biology
- Biophysics
Background:
- Amyloid protein toxicity is linked to cell membrane interactions.
- These interactions cause structural damage to both proteins and membranes.
- Membrane surfaces can accelerate the formation of toxic amyloid aggregates.
Purpose of the Study:
- To investigate the mechanisms by which amyloid-forming proteins interact with and disrupt cell membranes.
- To compare the membrane-disrupting effects of amyloid proteins with known toxins.
Main Methods:
- Utilized artificial model membranes to study protein-membrane interactions.
- Analyzed structural perturbations and membrane permeabilization.
Main Results:
- Amyloidogenic proteins and membranes mutually perturb each other's structures upon binding.
- Membrane surfaces promote the formation of toxic amyloid aggregates.
- Amyloid proteins compromise cell membrane integrity.
Conclusions:
- The toxicity of amyloid-forming proteins is directly related to their membrane interactions.
- Mechanisms of membrane permeabilization by amyloid proteins are similar to pore-forming toxins and antimicrobial peptides.
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