Cargando…

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...

Descripción completa

Detalles Bibliográficos
Autores principales: Kim, Gae Baik, Kim, Young-Pil
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Ivyspring International Publisher 2012
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
_version_ 1782224660587347968
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