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Few-layer bismuth selenides exfoliated by hemin inhibit amyloid-β(1–42) fibril formation
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,...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4446900/ https://www.ncbi.nlm.nih.gov/pubmed/26018135 http://dx.doi.org/10.1038/srep10171 |
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author | Peng, Jian Xiong, Yunjing Lin, Zhiqin Sun, Liping Weng, Jian |
author_facet | Peng, Jian Xiong, Yunjing Lin, Zhiqin Sun, Liping Weng, Jian |
author_sort | Peng, Jian |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-4446900 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-44469002015-06-10 Few-layer bismuth selenides exfoliated by hemin inhibit amyloid-β(1–42) fibril formation Peng, Jian Xiong, Yunjing Lin, Zhiqin Sun, Liping Weng, Jian Sci Rep Article 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. Nature Publishing Group 2015-05-28 /pmc/articles/PMC4446900/ /pubmed/26018135 http://dx.doi.org/10.1038/srep10171 Text en Copyright © 2015, Macmillan Publishers Limited http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ |
spellingShingle | Article Peng, Jian Xiong, Yunjing Lin, Zhiqin Sun, Liping Weng, Jian Few-layer bismuth selenides exfoliated by hemin inhibit amyloid-β(1–42) fibril formation |
title | Few-layer bismuth selenides exfoliated by hemin inhibit amyloid-β(1–42) fibril formation |
title_full | Few-layer bismuth selenides exfoliated by hemin inhibit amyloid-β(1–42) fibril formation |
title_fullStr | Few-layer bismuth selenides exfoliated by hemin inhibit amyloid-β(1–42) fibril formation |
title_full_unstemmed | Few-layer bismuth selenides exfoliated by hemin inhibit amyloid-β(1–42) fibril formation |
title_short | Few-layer bismuth selenides exfoliated by hemin inhibit amyloid-β(1–42) fibril formation |
title_sort | few-layer bismuth selenides exfoliated by hemin inhibit amyloid-β(1–42) fibril formation |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4446900/ https://www.ncbi.nlm.nih.gov/pubmed/26018135 http://dx.doi.org/10.1038/srep10171 |
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