Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 2019 Jan 23:14:799-808.
doi: 10.2147/IJN.S190354. eCollection 2019.

Effect of superparamagnetic nanoparticles coated with various electric charges on α-synuclein and β-amyloid proteins fibrillation process

Negin Javdani  1 , Sayyed Shahryar Rahpeyma  1 , Younes Ghasemi  2 , Jamshid Raheb  1
Affiliations

Effect of superparamagnetic nanoparticles coated with various electric charges on α-synuclein and β-amyloid proteins fibrillation process

Negin Javdani et al. Int J Nanomedicine. .

Erratum in

Abstract

Background: Most of nanoparticles are nontoxic and have high absorption capability. Therefore, nanoparticles binding can effectively restrain fibrillation of β-amyloid and α-synuclein proteins and eventually prevent the toxicity of pathogenesis peptide of Alzheimer. Super paramagnetic iron oxide nanoparticles (SPIONs) contain iron oxide core which can be connected to a special part through magnetic coating.

Materials and methods: In this study, the effect of SPIONs with different charges was simultaneously examined on the fibrillation of both β-amyloid and α-synuclein proteins by applying Thioflavin-T assay.

Results: According to the results of the investigation on amyloid-fibrillation mechanism in both β-amyloids and α-synucleins, it was revealed that negatively-charged nanoparticles encoded to -COOH by dextran-coating were able to have a considerable absorption decrease from 17,000-12,000 after 320 minutes delay to lag phase and decrease in binding level of thioflavin-T particles to β-sheets.

Conclusion: The different concentrations of these nanoparticles and special coating of each particle had an effect on the kinetics of β-amyloid and α-synuclein fibrillations.

Keywords: Alzheimer’s disease; Parkinson’s disease; SPION; fibrillation; α-synuclein; β-amyloid.

PubMed Disclaimer

Conflict of interest statement

Disclosure The authors report no conflicts of interest in this work.

Figures

Figure 1
Figure 1
Magnetic charge of iron nanoparticles. Notes: (A) Neutrally charged. (B) Positively charged. (C) Negatively charged.
Figure 2
Figure 2
Electronic microscope image of the effect of nanoparticles on fibrillation of Aβ-proteins. Notes: (A) fibrillation with no nanoparticle and (B) fibrillation with nanoparticle.
Figure 3
Figure 3
Diagram of SPIONs effect with a concentration of 2.5 µL and different charges on Aβ-protein fibrillation. Abbreviation: SPION, superparamagnetic iron-oxide nanoparticle.
Figure 4
Figure 4
Diagram of SPIONs effect with a concentration of 5 µL and different charges on Aβ-protein fibrillation. Abbreviation: SPION, superparamagnetic iron-oxide nanoparticle.
Figure 5
Figure 5
Diagram of SPIONs effect with a concentration of 10 µL and different charges on Aβ-protein fibrillation. Abbreviation: SPION, superparamagnetic iron-oxide nanoparticle.
Figure 6
Figure 6
Diagram of SPIONs effect with concentration of 2.5 µL and various charges on α-synuclein protein fibrillation. Abbreviation: SPION, superparamagnetic iron-oxide nanoparticle.
Figure 7
Figure 7
Diagram of SPIONs effect with concentration of 5 µL and various charges on α-synuclein protein fibrillation. Abbreviation: SPION, superparamagnetic iron-oxide nanoparticle.
Figure 8
Figure 8
Diagram of SPIONs effect with concentration of 10 µL and various charges on α-synuclein protein fibrillation. Abbreviation: SPION, superparamagnetic iron-oxide nanoparticle.
See this image and copyright information in PMC

References

    1. Fink AL. Protein aggregation: folding aggregates, inclusion bodies and amyloid. Fold Des. 1998;3(1):R9–R23. - PubMed
    1. Manno M, Mauro M, Craparo EF, Podest A, et al. Kinetics of different processes in human insulin amyloid formation. J Mol Biol. 2007;366(1):258–274. - PubMed
    1. Sherer TB, Kim JH, Betarbet R, Greenamyre JT. Subcutaneous rote-none exposure causes highly selective dopaminergic degeneration and α-synuclein aggregation. Experimental Neurology. 2003;179(1):9–16. - PubMed
    1. Cleary JP, Walsh DM, Hofmeister JJ, et al. Natural oligomers of the amyloid-beta protein specifically disrupt cognitive function. Nat Neurosci. 2005;8(1):79–84. - PubMed
    1. Walsh DM, Hartley DM, Kusumoto Y, et al. Amyloid beta-protein fibrillogenesis. Structure and biological activity of protofibrillar intermediates. J Biol Chem. 1999;274(36):25945–25952. - PubMed