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Nontoxic Black Phosphorus Quantum Dots Inhibit Insulin Amyloid Fibrillation at an Ultralow Concentration
Amyloid are protein aggregates formed by cross β structures assemblies. Inhibiting amyloid aggregation or facilitating its disassembly are considered to be two major effective therapeutic strategies in diseases involving peptide or protein fibrillation such Alzheimer's disease or diabetes. Usin...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7182724/ https://www.ncbi.nlm.nih.gov/pubmed/32334415 http://dx.doi.org/10.1016/j.isci.2020.101044 |
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author | Wang, Siqi Li, Chuanxi Xia, Yinqiang Chen, Shaohuang Robert, Jordan Banquy, Xavier Huang, Renliang Qi, Wei He, Zhimin Su, Rongxin |
author_facet | Wang, Siqi Li, Chuanxi Xia, Yinqiang Chen, Shaohuang Robert, Jordan Banquy, Xavier Huang, Renliang Qi, Wei He, Zhimin Su, Rongxin |
author_sort | Wang, Siqi |
collection | PubMed |
description | Amyloid are protein aggregates formed by cross β structures assemblies. Inhibiting amyloid aggregation or facilitating its disassembly are considered to be two major effective therapeutic strategies in diseases involving peptide or protein fibrillation such Alzheimer's disease or diabetes. Using thioflavin-T fluorescence, far-UV circular dichroism spectroscopy, and atomic force microscopy, we found nontoxic and biocompatible black phosphorus quantum dots (BPQDs) appear to have an exceptional capacity to inhibit insulin aggregation and to disassemble formed mature fibrils, even at an ultralow concentration (100 ng/mL). The inhibition of fibrillation persists at all stages of insulin aggregation and increases PC12 cells survival when exposed to amyloid fibrils. Molecular dynamics simulations suggest that BPQDs are able to stabilize the α-helix structure of insulin and obliterate the β-sheet structure to promote the fibril formation. These characteristics make BPQDs be promising candidate in preventing amyloidosis, disease treatment, as well as in the storage and processing of insulin. |
format | Online Article Text |
id | pubmed-7182724 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Elsevier |
record_format | MEDLINE/PubMed |
spelling | pubmed-71827242020-04-28 Nontoxic Black Phosphorus Quantum Dots Inhibit Insulin Amyloid Fibrillation at an Ultralow Concentration Wang, Siqi Li, Chuanxi Xia, Yinqiang Chen, Shaohuang Robert, Jordan Banquy, Xavier Huang, Renliang Qi, Wei He, Zhimin Su, Rongxin iScience Article Amyloid are protein aggregates formed by cross β structures assemblies. Inhibiting amyloid aggregation or facilitating its disassembly are considered to be two major effective therapeutic strategies in diseases involving peptide or protein fibrillation such Alzheimer's disease or diabetes. Using thioflavin-T fluorescence, far-UV circular dichroism spectroscopy, and atomic force microscopy, we found nontoxic and biocompatible black phosphorus quantum dots (BPQDs) appear to have an exceptional capacity to inhibit insulin aggregation and to disassemble formed mature fibrils, even at an ultralow concentration (100 ng/mL). The inhibition of fibrillation persists at all stages of insulin aggregation and increases PC12 cells survival when exposed to amyloid fibrils. Molecular dynamics simulations suggest that BPQDs are able to stabilize the α-helix structure of insulin and obliterate the β-sheet structure to promote the fibril formation. These characteristics make BPQDs be promising candidate in preventing amyloidosis, disease treatment, as well as in the storage and processing of insulin. Elsevier 2020-04-10 /pmc/articles/PMC7182724/ /pubmed/32334415 http://dx.doi.org/10.1016/j.isci.2020.101044 Text en © 2020 The Author(s) http://creativecommons.org/licenses/by-nc-nd/4.0/ This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/). |
spellingShingle | Article Wang, Siqi Li, Chuanxi Xia, Yinqiang Chen, Shaohuang Robert, Jordan Banquy, Xavier Huang, Renliang Qi, Wei He, Zhimin Su, Rongxin Nontoxic Black Phosphorus Quantum Dots Inhibit Insulin Amyloid Fibrillation at an Ultralow Concentration |
title | Nontoxic Black Phosphorus Quantum Dots Inhibit Insulin Amyloid Fibrillation at an Ultralow Concentration |
title_full | Nontoxic Black Phosphorus Quantum Dots Inhibit Insulin Amyloid Fibrillation at an Ultralow Concentration |
title_fullStr | Nontoxic Black Phosphorus Quantum Dots Inhibit Insulin Amyloid Fibrillation at an Ultralow Concentration |
title_full_unstemmed | Nontoxic Black Phosphorus Quantum Dots Inhibit Insulin Amyloid Fibrillation at an Ultralow Concentration |
title_short | Nontoxic Black Phosphorus Quantum Dots Inhibit Insulin Amyloid Fibrillation at an Ultralow Concentration |
title_sort | nontoxic black phosphorus quantum dots inhibit insulin amyloid fibrillation at an ultralow concentration |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7182724/ https://www.ncbi.nlm.nih.gov/pubmed/32334415 http://dx.doi.org/10.1016/j.isci.2020.101044 |
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