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Near-Infrared Aggregation-Induced Emission-Active Probe Enables in situ and Long-Term Tracking of Endogenous β-Galactosidase Activity
High-fidelity tracking of specific enzyme activities is critical for the early diagnosis of diseases such as cancers. However, most of the available fluorescent probes are difficult to obtain in situ information because of tending to facile diffusion or inevitably suffering from aggregation-caused q...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Frontiers Media S.A.
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6527754/ https://www.ncbi.nlm.nih.gov/pubmed/31139612 http://dx.doi.org/10.3389/fchem.2019.00291 |
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author | Fu, Wei Yan, Chenxu Zhang, Yutao Ma, Yiyu Guo, Zhiqian Zhu, Wei-Hong |
author_facet | Fu, Wei Yan, Chenxu Zhang, Yutao Ma, Yiyu Guo, Zhiqian Zhu, Wei-Hong |
author_sort | Fu, Wei |
collection | PubMed |
description | High-fidelity tracking of specific enzyme activities is critical for the early diagnosis of diseases such as cancers. However, most of the available fluorescent probes are difficult to obtain in situ information because of tending to facile diffusion or inevitably suffering from aggregation-caused quenching (ACQ) effect. In this work, we developed an elaborated near-infrared (NIR) aggregation-induced emission (AIE)-active fluorescent probe, which is composed of a hydrophobic 2-(2-hydroxyphenyl) benzothiazole (HBT) moiety for extending into the NIR wavelength, and a hydrophilic β-galactosidase (β-gal) triggered unit for improving miscibility and guaranteeing its non-emission in aqueous media. This probe is virtually activated by β-gal, and then specific enzymatic turnover would liberate hydrophobic AIE luminogen (AIEgen) QM-HBT-OH. Simultaneously, brightness NIR fluorescent nanoaggregates are in situ generated as a result of the AIE-active process, making on-site the detection of endogenous β-gal activity in living cells. By virtue of the NIR AIE-active performance of enzyme-catalyzed nanoaggregates, QM-HBT-βgal is capable of affording a localizable fluorescence signal and long-term tracking of endogenous β-gal activity. All results demonstrate that the probe QM-HBT-βgal has potential to be a powerful molecular tool to evaluate the biological activity of β-gal, attaining high-fidelity information in preclinical applications. |
format | Online Article Text |
id | pubmed-6527754 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-65277542019-05-28 Near-Infrared Aggregation-Induced Emission-Active Probe Enables in situ and Long-Term Tracking of Endogenous β-Galactosidase Activity Fu, Wei Yan, Chenxu Zhang, Yutao Ma, Yiyu Guo, Zhiqian Zhu, Wei-Hong Front Chem Chemistry High-fidelity tracking of specific enzyme activities is critical for the early diagnosis of diseases such as cancers. However, most of the available fluorescent probes are difficult to obtain in situ information because of tending to facile diffusion or inevitably suffering from aggregation-caused quenching (ACQ) effect. In this work, we developed an elaborated near-infrared (NIR) aggregation-induced emission (AIE)-active fluorescent probe, which is composed of a hydrophobic 2-(2-hydroxyphenyl) benzothiazole (HBT) moiety for extending into the NIR wavelength, and a hydrophilic β-galactosidase (β-gal) triggered unit for improving miscibility and guaranteeing its non-emission in aqueous media. This probe is virtually activated by β-gal, and then specific enzymatic turnover would liberate hydrophobic AIE luminogen (AIEgen) QM-HBT-OH. Simultaneously, brightness NIR fluorescent nanoaggregates are in situ generated as a result of the AIE-active process, making on-site the detection of endogenous β-gal activity in living cells. By virtue of the NIR AIE-active performance of enzyme-catalyzed nanoaggregates, QM-HBT-βgal is capable of affording a localizable fluorescence signal and long-term tracking of endogenous β-gal activity. All results demonstrate that the probe QM-HBT-βgal has potential to be a powerful molecular tool to evaluate the biological activity of β-gal, attaining high-fidelity information in preclinical applications. Frontiers Media S.A. 2019-05-14 /pmc/articles/PMC6527754/ /pubmed/31139612 http://dx.doi.org/10.3389/fchem.2019.00291 Text en Copyright © 2019 Fu, Yan, Zhang, Ma, Guo and Zhu. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Chemistry Fu, Wei Yan, Chenxu Zhang, Yutao Ma, Yiyu Guo, Zhiqian Zhu, Wei-Hong Near-Infrared Aggregation-Induced Emission-Active Probe Enables in situ and Long-Term Tracking of Endogenous β-Galactosidase Activity |
title | Near-Infrared Aggregation-Induced Emission-Active Probe Enables in situ and Long-Term Tracking of Endogenous β-Galactosidase Activity |
title_full | Near-Infrared Aggregation-Induced Emission-Active Probe Enables in situ and Long-Term Tracking of Endogenous β-Galactosidase Activity |
title_fullStr | Near-Infrared Aggregation-Induced Emission-Active Probe Enables in situ and Long-Term Tracking of Endogenous β-Galactosidase Activity |
title_full_unstemmed | Near-Infrared Aggregation-Induced Emission-Active Probe Enables in situ and Long-Term Tracking of Endogenous β-Galactosidase Activity |
title_short | Near-Infrared Aggregation-Induced Emission-Active Probe Enables in situ and Long-Term Tracking of Endogenous β-Galactosidase Activity |
title_sort | near-infrared aggregation-induced emission-active probe enables in situ and long-term tracking of endogenous β-galactosidase activity |
topic | Chemistry |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6527754/ https://www.ncbi.nlm.nih.gov/pubmed/31139612 http://dx.doi.org/10.3389/fchem.2019.00291 |
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