Se/Ru nanoparticles as inhibitors of metal-induced Aβ aggregation in Alzheimer's disease

Yang, Licong; Chen, Qingchang; Liu, Ying; Zhang, Jingnan; Sun, Dongdong; Zhou, Yanhui; Liu, Jie

doi:10.1039/c3tb21586e

Cited by 53 publications

(66 citation statements)

References 33 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Evidence from previous studies support the hypothesis that compounds or nanoparticles with high affinity to Aβ can prevent Aβ aggregation and neurotoxicity . Our previous research suggests that l ‐Cys‐modified Se/RuNPs is an effective inhibitor of metal ion induced Aβ40 aggregation due to its high binding affinity with Aβ40 . Therefore, nanoparticle interactions may offer a novel method to alter Aβ aggregation.…”

Section: Introductionsupporting

confidence: 53%

“…The fibrillation of Aβ42 was evaluated by dye Thioflavin T (ThT) . Briefly, 35 μM Aβ42 (dissolved in 50 mM PBS) incubated with 20, 40, and 60 μg/mL of Res@SeNPs or Res and 70 μM CuCl 2 from 0 to 5 days at 37°C.…”

Section: Methodsmentioning

confidence: 99%

“…Binding of nanoparticles on Aβ42 was confirmed by TEM according to the method of our previous investigation . Firstly, Aβ42 (35 μM) were incubated for 3 days to format the fibers.…”

Section: Methodsmentioning

confidence: 99%

“…However, limitations remain in the use of SeNPs in AD treatment. l ‐Cys‐modified SeNPs (Cys‐SeNPs) with low binding affinity to Aβ have been reported that can slightly inhibit Zn 2+ ‐induced Aβ40 fibril formation . This indicates that the binding of Aβ on SeNPs might affect metal ion induced Aβ aggregation.…”

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

A comparative study of resveratrol and resveratrol‐functional selenium nanoparticles: Inhibiting amyloid β aggregation and reactive oxygen species formation properties

Yang

Wang

Chen

et al. 2018

J Biomedical Materials Res

Self Cite

View full text Add to dashboard Cite

Deposition of amyloid‐β (Aβ) aggregates and formation of neurotoxic reactive oxygen species (ROS) are significant pathological signatures of Alzheimer's disease (AD). Resveratrol (Res) is an antioxidant with the potential to treat AD. However, the bioavailability and solubility of Res is very low and it cannot entirely inhibit Cu2+‐induced Aβ42 aggregation at low concentration. Herein, we combine the unique Aβ absorption property of selenium nanoparticles with the natural antioxidant agent Res to form Res@SeNPs. Our in vitro biological evaluation revealed that modification of Res with SeNPs provides a synergistic effect on Cu2+‐induced Aβ42 aggregation, ROS generation and, more importantly, protects PC12 cells from Aβ42–Cu2+ complexes‐induced cell death. It is believed that SeNPs can improve the application of Res in AD treatment as Res@SeNPs is more efficient than Res in reducing Aβ42 toxicity in long‐term use. © 2018 Wiley Periodicals, Inc. J Biomed Mater Res Part A: 106A: 3034–3041, 2018.

show abstract

Section: Introductionsupporting

confidence: 53%

Section: Methodsmentioning

confidence: 99%

“…Binding of nanoparticles on Aβ42 was confirmed by TEM according to the method of our previous investigation . Firstly, Aβ42 (35 μM) were incubated for 3 days to format the fibers.…”

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

A comparative study of resveratrol and resveratrol‐functional selenium nanoparticles: Inhibiting amyloid β aggregation and reactive oxygen species formation properties

Yang

Wang

Chen

et al. 2018

J Biomedical Materials Res

Self Cite

View full text Add to dashboard Cite

show abstract

“…They are probably involved in AD prevention, owing to their excellent neuroprotective property [20]. In recent years, the role of SeNPs and selenoproteins in neurodegenerative diseases has been studied [21,22]. With this background, we investigated the potential delivery efficiency and neuroprotective effects of SA-stabilised Se nanoparticles coated with B6 peptide (B6-SA-SeNPs) for the treatment of AD.…”

Section: Introductionmentioning

confidence: 99%

Sialic acid (SA)-modified selenium nanoparticles coated with a high blood–brain barrier permeability peptide-B6 peptide for potential use in Alzheimer’s disease

et al. 2015

Self Cite

View full text Add to dashboard Cite

The Design of Metal Complexes to Target the Amyloid‐β Peptide in Alzheimer's Disease

Webb

2023

Encyclopedia of Inorganic and Bioinorganic Chemistry

View full text Add to dashboard Cite

Alzheimer's disease (AD) is a devastating neurological disorder where a pathological hallmark is the occurrence of amyloid‐β (Aβ) peptide deposits, also known as Aβ plaques. The Aβ peptide is known to self‐associate and aggregate in solution, a phenomenon that is accelerated in the presence of metal ions, in particular Fe, Cu, and Zn. Furthermore, these micronutrient metals are found in elevated concentration within Aβ plaques, relative to nearby healthy tissues. Therapeutic approaches have sought to exploit this metalloprotein nature of Aβ by designing metal complexes that can target either the soluble peptide or its pathological aggregate species. Overall, complexes of 27 different metals have been designed to target the Aβ that can detect its presence in biological samples, modulate its aggregation, and/or prevent its neurotoxic activity. This article summarizes these compounds, and the advances made for complexes of each metal.

show abstract

Se/Ru nanoparticles as inhibitors of metal-induced Aβ aggregation in Alzheimer's disease

Cited by 53 publications

References 33 publications

A comparative study of resveratrol and resveratrol‐functional selenium nanoparticles: Inhibiting amyloid β aggregation and reactive oxygen species formation properties

A comparative study of resveratrol and resveratrol‐functional selenium nanoparticles: Inhibiting amyloid β aggregation and reactive oxygen species formation properties

Sialic acid (SA)-modified selenium nanoparticles coated with a high blood–brain barrier permeability peptide-B6 peptide for potential use in Alzheimer’s disease

The Design of Metal Complexes to Target the Amyloid‐β Peptide in Alzheimer's Disease

Contact Info

Product

Resources

About