&lt;p&gt;Effect of superparamagnetic nanoparticles coated with various electric charges on &amp;alpha;-synuclein and &amp;beta;-amyloid proteins fibrillation process&lt;/p&gt;

Javdani, Negin; Rahpeyma, Sayyed Shahryar; Ghasemi, Younes; Raheb, Jamshid

doi:10.2147/ijn.s190354

Cited by 24 publications

(5 citation statements)

References 28 publications

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“…Therefore, with the change of surface charge from positive to negative by some coatings, the level of protein aggregation or amyloid-fibrillation along with cytotoxicity can be greatly reduced. In this regard, Javdani, Rahpeyma, Ghasemi, Raheb43 exhibited that the change in the surface charge of iron NPs from positive to negative by dextran would reduce amyloid-fibrillation in both β-amyloids and α-syn.…”

Section: Discussionmentioning

confidence: 99%

<p>Cerium oxide NPs mitigate the amyloid formation of α-synuclein and associated cytotoxicity</p>

Zand¹,

Khaki²,

Salihi³

et al. 2019

IJN

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AimAmong therapeutic proposals for amyloid-associated disorders, special attention has been given to the exploitation of nanoparticles (NPs) as promising agents against aggregation.MethodsIn this paper, the inhibitory effect of cerium oxide (CeO2) NPs against α-synuclein (α-syn) amyloid formation was explored by different methods such as Thioflavin T (ThT) and 8-anilinonaphthalene-1-sulfonic acid (ANS) fluorescence spectroscopy, Congo red adsorption assay, circular dichroism (CD) spectroscopy, transmission electron microscopy (TEM), and bioinformatical approaches. Also, the cytotoxicity of α-syn amyloid either alone or with CeO2 NPs against neuron-like cells (SH-SY5Y) was examined using 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT), flow cytometry, and quantitative real-time polymerase chain reaction (Bax and Bcl-2 gene expression) assays.ResultsThT and ANS fluorescence assays indicated that CeO2 NPs inhibit the formation of aggregated species and hydrophobic patches of α-syn in amyloidogenic conditions, respectively. Congo red and CD assays demonstrated that CeO2 NPs reduce the formation of amyloid species and β-sheets structures of α-syn molecules, respectively. TEM investigation also confirmed that CeO2 NPs limited the formation of well-defined fibrillary structures of α-syn molecules. Molecular docking and dynamic studies revealed that CeO2 NPs could bind with different affinities to α-syn monomer and amyloid species and fibrillar structure of α-syn is disaggregated in the presence of CeO2 NPs. Moreover, cellular assays depicted that CeO2 NPs mitigate the cell mortality, apoptosis, and the ratio of Bax/Bcl-2 gene expression associated with α-syn amyloids.ConclusionIt may be concluded that CeO2 NPs can be used as therapeutic agents to reduce the aggregation of proteins and mitigate the occurrence of neurodegenerative diseases.

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Section: Discussionmentioning

confidence: 99%

<p>Cerium oxide NPs mitigate the amyloid formation of α-synuclein and associated cytotoxicity</p>

Zand¹,

Khaki²,

Salihi³

et al. 2019

IJN

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“…By applying thioflavin-T fluorescence emission, the effect of SPIONs with different electric charges on both β-amyloid and α-synuclein fibrillation process was investigated. The negatively charged nanoparticles encoded to -COOH by dextran-coating decreased the binding level of thioflavin-T particles to β-sheets (Javdani et al, 2019).…”

Section: Application Of Iron Oxide Nanoparticles In the Treatment Of Admentioning

confidence: 98%

Application of Iron Oxide Nanoparticles in the Diagnosis and Treatment of Neurodegenerative Diseases With Emphasis on Alzheimer’s Disease

Luo

Zhu

et al. 2020

Front. Cell. Neurosci.

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“…Some research groups have reported the use of NPs as a therapeutic approach to target amyloidosis. Recent data suggest that these nanomaterials can act as potential inhibitors of amyloid aggregation. − Moreover, it was observed that NPs had the ability to affect amyloid formation owing to their surface properties. Surface-coated NPs were first developed to increase their bioactivity and biocompatibility.…”

Section: Introductionmentioning

confidence: 99%

Dihydrocaffeic Acid-Decorated Iron Oxide Nanomaterials Effectively Inhibit Human Calcitonin Aggregation

Shen

Zhang

et al. 2022

ACS Omega

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To date, more than 30 human peptides or proteins have been found to form amyloid fibrils, most of which are associated with human diseases. However, currently, no cure for amyloidosis exists. Therefore, development of therapeutic strategies to inhibit amyloid formation is urgently required. Although the role of some amyloidogenic proteins has not been identified in certain diseases, their self-assembling behavior largely affects their bioactivity. Human calcitonin (hCT) is a hormone peptide containing 32 amino acids and is secreted by the parafollicular cells of the thyroid gland in the human body. It can regulate the concentration of calcium ions in the blood and block the activity of osteoclasts. Therefore, calcitonin has also been considered a therapeutic peptide. However, the aggregation of hCT hinders this process, and hCT has been replaced by salmon calcitonin in drug formulations. Recently, iron oxide nanomaterials have been developed as potential materials for various applications owing to their high biocompatibility, low toxicity, and ease of functionalization. In this study, nanoparticles (NPs) were prepared using a simple chemical coprecipitation method. We first demonstrated that dopamine-conjugated Fe 3 O 4 inhibited hCT aggregation, similar to what we found when carbon dots were used as core materials in the previous study. Later, we continued to simplify the preparation process, that is, the mixing of dihydrocaffeic acid (DCA) and iron oxide NPs, to maintain their stability and inhibitory effect against hCT aggregation. Furthermore, DCA-decorated Fe 3 O 4 can dissociate preformed hCT amyloid fibrils. This appears to be one of the most promising ways to stabilize hCT in solution and may be helpful for amyloidosis treatment.

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

Cited by 24 publications

References 28 publications

<p>Cerium oxide NPs mitigate the amyloid formation of α-synuclein and associated cytotoxicity</p>

<p>Cerium oxide NPs mitigate the amyloid formation of α-synuclein and associated cytotoxicity</p>

Application of Iron Oxide Nanoparticles in the Diagnosis and Treatment of Neurodegenerative Diseases With Emphasis on Alzheimer’s Disease

Dihydrocaffeic Acid-Decorated Iron Oxide Nanomaterials Effectively Inhibit Human Calcitonin Aggregation

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