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Analysis of Protease Activity Using Quantum Dots and Resonance Energy Transfer
This review demonstrates the detection of protease activity based on the energy transfer of quantum dots (QDs). By incorporation of varying protease substrates into designed QD probes both in fluorescence resonance energy transfer (FRET) and bioluminescence resonance energy transfer (BRET) system, p...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Ivyspring International Publisher
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3287427/ https://www.ncbi.nlm.nih.gov/pubmed/22375154 http://dx.doi.org/10.7150/thno.3476 |
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author | Kim, Gae Baik Kim, Young-Pil |
author_facet | Kim, Gae Baik Kim, Young-Pil |
author_sort | Kim, Gae Baik |
collection | PubMed |
description | This review demonstrates the detection of protease activity based on the energy transfer of quantum dots (QDs). By incorporation of varying protease substrates into designed QD probes both in fluorescence resonance energy transfer (FRET) and bioluminescence resonance energy transfer (BRET) system, proteolytic activity led to changes in the energy transfer efficiency. Especially due to the superior properties of QDs, it can be served as an excellent probe for a multiplexed and high-throughput protease assay with high sensitivity. It is anticipated that the QD-based FRET/BRET probes will have a great potential for dissecting the fundamental roles of proteases and designing potential protease inhibitors as therapeutic drugs in biology and nanomedicine. |
format | Online Article Text |
id | pubmed-3287427 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | Ivyspring International Publisher |
record_format | MEDLINE/PubMed |
spelling | pubmed-32874272012-02-28 Analysis of Protease Activity Using Quantum Dots and Resonance Energy Transfer Kim, Gae Baik Kim, Young-Pil Theranostics Review This review demonstrates the detection of protease activity based on the energy transfer of quantum dots (QDs). By incorporation of varying protease substrates into designed QD probes both in fluorescence resonance energy transfer (FRET) and bioluminescence resonance energy transfer (BRET) system, proteolytic activity led to changes in the energy transfer efficiency. Especially due to the superior properties of QDs, it can be served as an excellent probe for a multiplexed and high-throughput protease assay with high sensitivity. It is anticipated that the QD-based FRET/BRET probes will have a great potential for dissecting the fundamental roles of proteases and designing potential protease inhibitors as therapeutic drugs in biology and nanomedicine. Ivyspring International Publisher 2012-02-01 /pmc/articles/PMC3287427/ /pubmed/22375154 http://dx.doi.org/10.7150/thno.3476 Text en © Ivyspring International Publisher. This is an open-access article distributed under the terms of the Creative Commons License (http://creativecommons.org/licenses/by-nc-nd/3.0/). Reproduction is permitted for personal, noncommercial use, provided that the article is in whole, unmodified, and properly cited. |
spellingShingle | Review Kim, Gae Baik Kim, Young-Pil Analysis of Protease Activity Using Quantum Dots and Resonance Energy Transfer |
title | Analysis of Protease Activity Using Quantum Dots and Resonance Energy Transfer |
title_full | Analysis of Protease Activity Using Quantum Dots and Resonance Energy Transfer |
title_fullStr | Analysis of Protease Activity Using Quantum Dots and Resonance Energy Transfer |
title_full_unstemmed | Analysis of Protease Activity Using Quantum Dots and Resonance Energy Transfer |
title_short | Analysis of Protease Activity Using Quantum Dots and Resonance Energy Transfer |
title_sort | analysis of protease activity using quantum dots and resonance energy transfer |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3287427/ https://www.ncbi.nlm.nih.gov/pubmed/22375154 http://dx.doi.org/10.7150/thno.3476 |
work_keys_str_mv | AT kimgaebaik analysisofproteaseactivityusingquantumdotsandresonanceenergytransfer AT kimyoungpil analysisofproteaseactivityusingquantumdotsandresonanceenergytransfer |