Related Experiment Video
Updated: May 6, 2026
15:04
Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils
Published on: September 28, 2019
5.3K
Probing the interplay between amyloidogenic proteins and membranes using lipid monolayers and bilayers
Annalisa Relini1, Nadia Marano2, Alessandra Gliozzi3
1Department of Physics, University of Genoa, Genoa, Italy; Research Centre on the Molecular Basis of Neurodegeneration, Florence, Italy.
Advances in Colloid and Interface Science
|November 9, 2013
Summary
Membrane interactions accelerate amyloid protein aggregation and fiber formation, contributing to neurodegenerative diseases like Alzheimer's. These interactions also damage cell membranes through various permeabilization mechanisms.
Area of Science:
- Biochemistry
- Biophysics
- Neuroscience
Background:
- Neurodegenerative diseases like Alzheimer's and Parkinson's are linked to protein misfolding and amyloid fiber formation.
- Cell membranes play a critical role in modulating these protein aggregation processes.
Purpose of the Study:
- To review how model membrane systems elucidate amyloidogenic protein-membrane interactions.
- To explore the dual role of membranes in promoting aggregation and causing damage.
Main Methods:
- Utilizing model membrane systems: monolayers, bilayers, supported membranes, and vesicles.
- Analyzing interfacial effects, including surface charge and lipid composition (anionic lipids, rafts).
- Examining various membrane permeabilization models (pores, lipid extraction, tension).
Main Results:
- Interfaces, particularly charged ones, enhance protein aggregation by increasing effective concentration and enabling electrostatic interactions.
- Specific lipid compositions (anionic lipids, cholesterol/ganglioside-rich rafts) are crucial.
- Membrane damage occurs via mechanisms including protein pores, lipid extraction, chaotic pores, and membrane tension.
Conclusions:
- Membrane environment significantly influences amyloidogenic protein aggregation and subsequent membrane damage.
- The predominant damage mechanism is protein- and lipid environment-dependent.
Related Concept Videos
01:35Asymmetric Lipid Bilayer
8.1K
Biological membranes show uneven distribution of different types of lipids in the inner and outer layers, resulting in transverse asymmetric membranes. The treatment of the erythrocyte membrane with the enzyme phospholipase confirmed the asymmetric nature of the lipid bilayer. The enzyme hydrolyzes lipids into fatty acids and hydrophilic groups. The phospholipase acts only on the outer layer of the membrane, while the inner layer remains intact. The phospholipase treatment resulted in 80%...
8.1K
03:03Amyloid Fibrils
10.3K
Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils.
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...
10.3K