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Published on: September 12, 2019
Interaction Dynamics in Inhibiting the Aggregation of Aβ Peptides by SWCNTs: A Combined Experimental and
Dongdong Lin1, Ruxi Qi1, Shujie Li1
1State Key Laboratory of Surface Physics and Key Laboratory for Computational Physical, Fudan University , Shanghai 200433, China.
Abstract:
The aggregation of amyloid-β peptides (Aβ) is considered as the main possible cause of Alzheimer's disease (AD). How to suppress the formation of toxic Aβ aggregates has been an intensive concern over the past several decades. Increasing evidence shows that whether carbon nanomaterials can suppress or promote the aggregation depends on their physicochemical properties. However, their interaction dynamics remains elusive as amyloid fibrillation is a complex multistep process. In this paper, we utilized atomic force microscopy (AFM), electrostatic force microscopy (EFM), ThT/fluorescence spectroscopy, and cell viability measurements, combined with coarse-grained molecular dynamic (MD) simulations to study the dynamic interaction of full length Aβ with single-walled carbon nanotubes (SWCNT). At the single SWCNTs scale, it is found that the presence of SWCNTs would result in rapid and spontaneous adsorption of Aβ1-40 peptides on their surface and stacking into nonfibrillar aggregates with reduced toxicity, which plays an important role in inhibiting the formation of toxic oligomers and mature fibrils. Our results provide new clues for studying the interaction in amyloid/SWCNTs system as well as for seeking amyloidosis inhibitors with carbon nanomaterials.
Insights
Single-walled carbon nanotubes (SWCNTs) reduce Alzheimer's disease peptide (Aβ) aggregation. SWCNTs promote non-toxic Aβ stacking, inhibiting harmful fibril formation and reducing peptide toxicity.
Area of Science:
- Biochemistry
- Nanotechnology
- Neuroscience
Background:
- Amyloid-β (Aβ) peptide aggregation is a key factor in Alzheimer's disease (AD) pathogenesis.
- Controlling Aβ aggregation is crucial for developing AD therapies.
- Carbon nanomaterials' effects on Aβ aggregation depend on their properties, but interaction dynamics are unclear.
Purpose of the Study:
- To investigate the dynamic interactions between full-length Aβ peptides and single-walled carbon nanotubes (SWCNTs).
- To understand how SWCNTs influence Aβ aggregation pathways and toxicity.
Main Methods:
- Atomic force microscopy (AFM) and electrostatic force microscopy (EFM).
- Thioflavin T (ThT)/fluorescence spectroscopy.
- Cell viability assays.
- Coarse-grained molecular dynamics (MD) simulations.
Main Results:
- SWCNTs induce rapid, spontaneous adsorption of Aβ1-40 peptides onto their surface.
- Aβ peptides on SWCNTs form non-fibrillar aggregates with reduced toxicity.
- This process inhibits the formation of toxic Aβ oligomers and mature fibrils.
Conclusions:
- SWCNTs can act as inhibitors of toxic amyloid-β aggregation.
- Understanding Aβ/SWCNT interactions offers insights for developing novel amyloidosis inhibitors using carbon nanomaterials.
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