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Conjugated Quantum Dots Inhibit the Amyloid β (1–42) Fibrillation Process
Nanoparticles have enormous potential in diagnostic and therapeutic studies. We have demonstrated that the amyloid beta mixed with and conjugated to dihydrolipoic acid- (DHLA) capped CdSe/ZnS quantum dots (QDs) of size approximately 2.5 nm can be used to reduce the fibrillation process. Transmission...
Autores principales: | , , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
SAGE-Hindawi Access to Research
2011
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3056432/ https://www.ncbi.nlm.nih.gov/pubmed/21423556 http://dx.doi.org/10.4061/2011/502386 |
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author | Thakur, Garima Micic, Miodrag Yang, Yuehai Li, Wenzhi Movia, Dania Giordani, Silvia Zhang, Hongzhou Leblanc, Roger M. |
author_facet | Thakur, Garima Micic, Miodrag Yang, Yuehai Li, Wenzhi Movia, Dania Giordani, Silvia Zhang, Hongzhou Leblanc, Roger M. |
author_sort | Thakur, Garima |
collection | PubMed |
description | Nanoparticles have enormous potential in diagnostic and therapeutic studies. We have demonstrated that the amyloid beta mixed with and conjugated to dihydrolipoic acid- (DHLA) capped CdSe/ZnS quantum dots (QDs) of size approximately 2.5 nm can be used to reduce the fibrillation process. Transmission electron microscopy (TEM) and atomic force microscopy (AFM) were used as tools for analysis of fibrillation. There is a significant change in morphology of fibrils when amyloid β (1–42) (Aβ (1–42)) is mixed or conjugated to the QDs. The length and the width of the fibrils vary under modified conditions. Thioflavin T (ThT) fluorescence supports the decrease in fibril formation in presence of DHLA-capped QDs. |
format | Text |
id | pubmed-3056432 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | SAGE-Hindawi Access to Research |
record_format | MEDLINE/PubMed |
spelling | pubmed-30564322011-03-21 Conjugated Quantum Dots Inhibit the Amyloid β (1–42) Fibrillation Process Thakur, Garima Micic, Miodrag Yang, Yuehai Li, Wenzhi Movia, Dania Giordani, Silvia Zhang, Hongzhou Leblanc, Roger M. Int J Alzheimers Dis Research Article Nanoparticles have enormous potential in diagnostic and therapeutic studies. We have demonstrated that the amyloid beta mixed with and conjugated to dihydrolipoic acid- (DHLA) capped CdSe/ZnS quantum dots (QDs) of size approximately 2.5 nm can be used to reduce the fibrillation process. Transmission electron microscopy (TEM) and atomic force microscopy (AFM) were used as tools for analysis of fibrillation. There is a significant change in morphology of fibrils when amyloid β (1–42) (Aβ (1–42)) is mixed or conjugated to the QDs. The length and the width of the fibrils vary under modified conditions. Thioflavin T (ThT) fluorescence supports the decrease in fibril formation in presence of DHLA-capped QDs. SAGE-Hindawi Access to Research 2011-03-02 /pmc/articles/PMC3056432/ /pubmed/21423556 http://dx.doi.org/10.4061/2011/502386 Text en Copyright © 2011 Garima Thakur et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Article Thakur, Garima Micic, Miodrag Yang, Yuehai Li, Wenzhi Movia, Dania Giordani, Silvia Zhang, Hongzhou Leblanc, Roger M. Conjugated Quantum Dots Inhibit the Amyloid β (1–42) Fibrillation Process |
title | Conjugated Quantum Dots Inhibit the Amyloid β (1–42) Fibrillation Process |
title_full | Conjugated Quantum Dots Inhibit the Amyloid β (1–42) Fibrillation Process |
title_fullStr | Conjugated Quantum Dots Inhibit the Amyloid β (1–42) Fibrillation Process |
title_full_unstemmed | Conjugated Quantum Dots Inhibit the Amyloid β (1–42) Fibrillation Process |
title_short | Conjugated Quantum Dots Inhibit the Amyloid β (1–42) Fibrillation Process |
title_sort | conjugated quantum dots inhibit the amyloid β (1–42) fibrillation process |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3056432/ https://www.ncbi.nlm.nih.gov/pubmed/21423556 http://dx.doi.org/10.4061/2011/502386 |
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