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Updated: Feb 23, 2026
Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils
Published on: September 28, 2019
Amyloid and membrane complexity: The toxic interplay revealed by AFM
Claudio Canale1, Reinier Oropesa-Nuñez2, Alberto Diaspro1
1Department of Nanophysics. Istituto Italiano di Tecnologia. Via Morego 30, 16163 Genova, Italy; Department of Physics, University of Genova, via Dodecaneso 33, 16146 Genova, Italy.
Abstract:
Lipid membranes play a fundamental role in the pathological development of protein misfolding diseases. Several pieces of evidence suggest that the lipid membrane could act as a catalytic surface for protein aggregation. Furthermore, a leading theory indicates the interaction between the cell membrane and misfolded oligomer species as the responsible for cytotoxicity, hence, for neurodegeneration in disorders such as Alzheimer's and Parkinson's disease. The definition of the mechanisms that drive the interaction between pathological protein aggregates and plasma membrane is fundamental for the development of effective therapies for a large class of diseases. Atomic force microscopy (AFM) has been employed to study how amyloid aggregates affect the cell physiological properties. Considerable efforts were spent to characterize the interaction with model systems, i.e., planar supported lipid bilayers, but some works also addressed the problem directly on living cells. Here, an overview of the main works involving the use of the AFM on both model system and living cells will be provided. Different kind of approaches will be presented, as well as the main results derived from the AFM analysis.
Insights
Lipid membranes are key in protein misfolding diseases like Alzheimer's. Atomic force microscopy (AFM) reveals how amyloid aggregates interact with cell membranes, offering insights for new therapies.
Area of Science:
- Biophysics
- Cell Biology
- Neuroscience
Background:
- Lipid membranes are implicated in protein misfolding diseases.
- Cell membrane interaction with misfolded proteins causes cytotoxicity and neurodegeneration.
- Understanding these interactions is crucial for developing therapies for Alzheimer's and Parkinson's disease.
Purpose of the Study:
- To provide an overview of Atomic Force Microscopy (AFM) applications in studying protein aggregate-membrane interactions.
- To present various AFM approaches used on both model systems and living cells.
- To summarize key findings from AFM analyses in this field.
Main Methods:
- Atomic Force Microscopy (AFM) was used to investigate the effects of amyloid aggregates on cellular properties.
- Studies were conducted on model systems, specifically planar supported lipid bilayers.
- AFM was also applied directly to living cells to study these interactions in a more complex environment.
Main Results:
- AFM has been instrumental in characterizing the interaction between amyloid aggregates and lipid membranes.
- Distinct AFM approaches have yielded insights into the mechanisms driving these interactions.
- Results from both model systems and living cells provide a comprehensive understanding of aggregate-membrane dynamics.
Conclusions:
- AFM is a powerful tool for dissecting the role of lipid membranes in protein misfolding diseases.
- Characterizing the interaction between pathological protein aggregates and plasma membranes is fundamental for therapeutic development.
- Further research using AFM can lead to novel therapeutic strategies for neurodegenerative disorders.
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03:03Amyloid Fibrils
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...
03:03Amyloid Fibrils