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Fullerenes as an Effective Amyloid Fibrils Disaggregating Nanomaterial
Katarina Siposova1,2, Viktor I Petrenko3,4, Oleksandr I Ivankov2,5
1Department of Biophysics, Institute of Experimental Physics, Slovak Academy of Sciences, Watsonova 47, 04001 Kosice, Slovakia.
ACS Applied Materials & Interfaces
|June 30, 2020
Summary
Fullerenes C60 and C70 effectively break down amyloid fibrils from lysozyme and insulin. This research offers insights into fullerene nanomaterials for treating amyloid-related diseases.
Area of Science:
- Biochemistry
- Materials Science
- Nanotechnology
Background:
- Amyloid fibrils are implicated in neurodegenerative diseases.
- Understanding amyloid disassembly is crucial for therapeutic development.
- Nanomaterials show potential for targeting amyloid aggregates.
Purpose of the Study:
- To investigate the amyloid disassembly activity of fullerene C60 and C70 complexes.
- To explore the mechanism by which fullerenes interact with and break down amyloid fibrils.
- To assess the therapeutic potential of fullerene-based agents for amyloid-related diseases.
Main Methods:
- Thioflavin T fluorescence assay to monitor disaggregation.
- Atomic force microscopy to visualize fibril changes.
- Small-angle neutron scattering to analyze aggregate structure and morphology.
Main Results:
- Fullerene C60 and C70 complexes effectively disassembled preformed amyloid fibrils.
- Low apparent half-maximal disaggregation concentrations (DC50) of ~22-30 μg mL−1 were observed.
- Small-angle neutron scattering provided insights into the stages of the disassembly process.
Conclusions:
- Fullerene/NMP complexes are potent agents for amyloid fibril disassembly.
- A mechanism for fullerene-mediated amyloid disassembly has been proposed.
- This study provides a foundation for engineering macromolecules to combat amyloid diseases.
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