Limits...
Few-layer bismuth selenides exfoliated by hemin inhibit amyloid-β1-42 fibril formation.

Peng J, Xiong Y, Lin Z, Sun L, Weng J - Sci Rep (2015)

Bottom Line: The results show that smaller and thinner few-layer Bi(2)Se(3) had the highest inhibition efficiency.The results indicate that the inhibition effect may be due to the high adsorption capacity of few-layer Bi(2)Se(3) for Aβ(1-42) monomers.Few-layer Bi(2)Se(3) also decreased Aβ-mediated peroxidase-like activity and cytotoxicity according to in vitro neurotoxicity studies under physiological conditions.

View Article: PubMed Central - PubMed

Affiliation: 1] College of Chemistry and Chemical Engineering, Xiamen University, Xiamen 361005, P.R. China [2] College of Materials, Xiamen University, Xiamen 361005, P.R. China.

ABSTRACT
Inhibiting amyloid-β (Aβ) fibril formation is the primary therapeutic strategy for Alzheimer's disease. Several small molecules and nanomaterials have been used to inhibit Aβ fibril formation. However, insufficient inhibition efficiency or poor metabolization limits their further applications. Here, we used hemin to exfoliate few-layer Bi(2)Se(3) in aqueous solution. Then we separated few-layer Bi(2)Se(3) with different sizes and thicknesses by fractional centrifugation, and used them to attempt to inhibit Aβ(1-42) aggregation. The results show that smaller and thinner few-layer Bi(2)Se(3) had the highest inhibition efficiency. We further investigated the interaction between few-layer Bi(2)Se(3) and Aβ(1-42) monomers. The results indicate that the inhibition effect may be due to the high adsorption capacity of few-layer Bi(2)Se(3) for Aβ(1-42) monomers. Few-layer Bi(2)Se(3) also decreased Aβ-mediated peroxidase-like activity and cytotoxicity according to in vitro neurotoxicity studies under physiological conditions. Therefore, our work shows the potential for applications of few-layer Bi(2)Se(3) in the biomedical field.

No MeSH data available.


Related in: MedlinePlus

Few-layer Bi2Se3 reduces the cytoxicity induced by Aβ1-42 fibrils for C6 rat glioma cells. Samples were prepared in the presence (a) or absence (b) of Aβ1-42. The cytotoxic effect on C6 cells was determined by MTT assay from three separate measurements. Error bars indicate±s.d. Percentage of cytotoxicity was calculated as follows: Cytotoxicity = 100% - cell viability.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
getmorefigures.php?uid=PMC4446900&req=5

f8: Few-layer Bi2Se3 reduces the cytoxicity induced by Aβ1-42 fibrils for C6 rat glioma cells. Samples were prepared in the presence (a) or absence (b) of Aβ1-42. The cytotoxic effect on C6 cells was determined by MTT assay from three separate measurements. Error bars indicate±s.d. Percentage of cytotoxicity was calculated as follows: Cytotoxicity = 100% - cell viability.

Mentions: To assess the cytoxicity effect of few-layer Bi2Se3-induced Aβ1-42 species, we performed 3-[4,5-Dimethylthiazol-2-yl]-2,5-diphenyltetrazdium bromide (MTT) assays to examine the activity of mitochondrial alcohol dehydrogenase by treating rat glioma cells, C6, with our end-point products at 3 h. Cytoxicity was demonstrated by the reduction of cell viability and the viability is normalized to the one treated with the buffer control. Aβ1-42 fibril alone contributed to ~22% cytoxicity to the glioma cells (Fig. 8a). For the end-point products obtained from Aβ1-42 monomer incubated with few-layer Bi2Se3 with different concentrations, the cytoxicity decreased with increasing concentration of few-layer Bi2Se3 in a dose-dependent manner. When few-layer Bi2Se3 concentration was 1200 ng mL-1, the cytotoxicity was significantly reduced to ~7%. Furthermore, the toxicity of few-layer Bi2Se3 itself was evaluated by MTT assay (Fig. 8b). Few-layer Bi2Se3 itself with the concentration used above showed little cell toxicity under our experiment conditions. These results suggest that few-layer Bi2Se3 can inhibit Aβ1-42-induced cell toxicity.


Few-layer bismuth selenides exfoliated by hemin inhibit amyloid-β1-42 fibril formation.

Peng J, Xiong Y, Lin Z, Sun L, Weng J - Sci Rep (2015)

Few-layer Bi2Se3 reduces the cytoxicity induced by Aβ1-42 fibrils for C6 rat glioma cells. Samples were prepared in the presence (a) or absence (b) of Aβ1-42. The cytotoxic effect on C6 cells was determined by MTT assay from three separate measurements. Error bars indicate±s.d. Percentage of cytotoxicity was calculated as follows: Cytotoxicity = 100% - cell viability.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4446900&req=5

f8: Few-layer Bi2Se3 reduces the cytoxicity induced by Aβ1-42 fibrils for C6 rat glioma cells. Samples were prepared in the presence (a) or absence (b) of Aβ1-42. The cytotoxic effect on C6 cells was determined by MTT assay from three separate measurements. Error bars indicate±s.d. Percentage of cytotoxicity was calculated as follows: Cytotoxicity = 100% - cell viability.
Mentions: To assess the cytoxicity effect of few-layer Bi2Se3-induced Aβ1-42 species, we performed 3-[4,5-Dimethylthiazol-2-yl]-2,5-diphenyltetrazdium bromide (MTT) assays to examine the activity of mitochondrial alcohol dehydrogenase by treating rat glioma cells, C6, with our end-point products at 3 h. Cytoxicity was demonstrated by the reduction of cell viability and the viability is normalized to the one treated with the buffer control. Aβ1-42 fibril alone contributed to ~22% cytoxicity to the glioma cells (Fig. 8a). For the end-point products obtained from Aβ1-42 monomer incubated with few-layer Bi2Se3 with different concentrations, the cytoxicity decreased with increasing concentration of few-layer Bi2Se3 in a dose-dependent manner. When few-layer Bi2Se3 concentration was 1200 ng mL-1, the cytotoxicity was significantly reduced to ~7%. Furthermore, the toxicity of few-layer Bi2Se3 itself was evaluated by MTT assay (Fig. 8b). Few-layer Bi2Se3 itself with the concentration used above showed little cell toxicity under our experiment conditions. These results suggest that few-layer Bi2Se3 can inhibit Aβ1-42-induced cell toxicity.

Bottom Line: The results show that smaller and thinner few-layer Bi(2)Se(3) had the highest inhibition efficiency.The results indicate that the inhibition effect may be due to the high adsorption capacity of few-layer Bi(2)Se(3) for Aβ(1-42) monomers.Few-layer Bi(2)Se(3) also decreased Aβ-mediated peroxidase-like activity and cytotoxicity according to in vitro neurotoxicity studies under physiological conditions.

View Article: PubMed Central - PubMed

Affiliation: 1] College of Chemistry and Chemical Engineering, Xiamen University, Xiamen 361005, P.R. China [2] College of Materials, Xiamen University, Xiamen 361005, P.R. China.

ABSTRACT
Inhibiting amyloid-β (Aβ) fibril formation is the primary therapeutic strategy for Alzheimer's disease. Several small molecules and nanomaterials have been used to inhibit Aβ fibril formation. However, insufficient inhibition efficiency or poor metabolization limits their further applications. Here, we used hemin to exfoliate few-layer Bi(2)Se(3) in aqueous solution. Then we separated few-layer Bi(2)Se(3) with different sizes and thicknesses by fractional centrifugation, and used them to attempt to inhibit Aβ(1-42) aggregation. The results show that smaller and thinner few-layer Bi(2)Se(3) had the highest inhibition efficiency. We further investigated the interaction between few-layer Bi(2)Se(3) and Aβ(1-42) monomers. The results indicate that the inhibition effect may be due to the high adsorption capacity of few-layer Bi(2)Se(3) for Aβ(1-42) monomers. Few-layer Bi(2)Se(3) also decreased Aβ-mediated peroxidase-like activity and cytotoxicity according to in vitro neurotoxicity studies under physiological conditions. Therefore, our work shows the potential for applications of few-layer Bi(2)Se(3) in the biomedical field.

No MeSH data available.


Related in: MedlinePlus