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Addition of a Second Binding Site Increases the Dynamic Range but Alters the Cellular Localization of a Red Fluorescent Probe for Mobile Zinc
[Image: see text] We report the synthesis and photophysical properties of ZBR4 and ZR1, two resorufin-based ditopic probes for mobile zinc. Upon binding Zn(2+), the sensors display 14- and 41-fold enhancements of their red fluorescence emission, respectively. In contrast to ZR1 and other members of...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical Society
2014
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4095928/ https://www.ncbi.nlm.nih.gov/pubmed/24915285 http://dx.doi.org/10.1021/ic500732z |
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author | Loas, Andrei Radford, Robert J. Lippard, Stephen J. |
author_facet | Loas, Andrei Radford, Robert J. Lippard, Stephen J. |
author_sort | Loas, Andrei |
collection | PubMed |
description | [Image: see text] We report the synthesis and photophysical properties of ZBR4 and ZR1, two resorufin-based ditopic probes for mobile zinc. Upon binding Zn(2+), the sensors display 14- and 41-fold enhancements of their red fluorescence emission, respectively. In contrast to ZR1 and other members of the ZBR family, which accumulate in the endoplasmic reticulum, ZBR4 spontaneously localizes to the mitochondria of HeLa cells. The modular approach in designing the constructs facilitates a homologation strategy aimed at tuning the zinc-binding and intracellular targeting properties of future probes. |
format | Online Article Text |
id | pubmed-4095928 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | American Chemical Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-40959282014-07-24 Addition of a Second Binding Site Increases the Dynamic Range but Alters the Cellular Localization of a Red Fluorescent Probe for Mobile Zinc Loas, Andrei Radford, Robert J. Lippard, Stephen J. Inorg Chem [Image: see text] We report the synthesis and photophysical properties of ZBR4 and ZR1, two resorufin-based ditopic probes for mobile zinc. Upon binding Zn(2+), the sensors display 14- and 41-fold enhancements of their red fluorescence emission, respectively. In contrast to ZR1 and other members of the ZBR family, which accumulate in the endoplasmic reticulum, ZBR4 spontaneously localizes to the mitochondria of HeLa cells. The modular approach in designing the constructs facilitates a homologation strategy aimed at tuning the zinc-binding and intracellular targeting properties of future probes. American Chemical Society 2014-06-10 2014-07-07 /pmc/articles/PMC4095928/ /pubmed/24915285 http://dx.doi.org/10.1021/ic500732z Text en Copyright © 2014 American Chemical Society Terms of Use (http://pubs.acs.org/page/policy/authorchoice_termsofuse.html) |
spellingShingle | Loas, Andrei Radford, Robert J. Lippard, Stephen J. Addition of a Second Binding Site Increases the Dynamic Range but Alters the Cellular Localization of a Red Fluorescent Probe for Mobile Zinc |
title | Addition of a Second Binding Site Increases the Dynamic Range but Alters the Cellular
Localization of a Red Fluorescent Probe for Mobile Zinc |
title_full | Addition of a Second Binding Site Increases the Dynamic Range but Alters the Cellular
Localization of a Red Fluorescent Probe for Mobile Zinc |
title_fullStr | Addition of a Second Binding Site Increases the Dynamic Range but Alters the Cellular
Localization of a Red Fluorescent Probe for Mobile Zinc |
title_full_unstemmed | Addition of a Second Binding Site Increases the Dynamic Range but Alters the Cellular
Localization of a Red Fluorescent Probe for Mobile Zinc |
title_short | Addition of a Second Binding Site Increases the Dynamic Range but Alters the Cellular
Localization of a Red Fluorescent Probe for Mobile Zinc |
title_sort | addition of a second binding site increases the dynamic range but alters the cellular
localization of a red fluorescent probe for mobile zinc |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4095928/ https://www.ncbi.nlm.nih.gov/pubmed/24915285 http://dx.doi.org/10.1021/ic500732z |
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