Design, Synthesis, and Biological Application of Fluorescent Sensor Molecules for Cellular Imaging

2009 ◽  
pp. 63-78 ◽  
Author(s):  
Kazuya Kikuchi
2018 ◽  
Vol 26 (20) ◽  
pp. 5510-5530 ◽  
Author(s):  
Tom Baladi ◽  
Jessy Aziz ◽  
Florent Dufour ◽  
Valentina Abet ◽  
Véronique Stoven ◽  
...  

2011 ◽  
Vol 21 (11) ◽  
pp. 3858-3862 ◽  
Author(s):  
Wei Shen ◽  
Shaobo Long ◽  
Shian Yu ◽  
Weiwei Chen ◽  
Qing Zhu

2020 ◽  
Author(s):  
Regina A. Baglia ◽  
Kira Mills ◽  
Koushambi Mitra ◽  
Jasmine Tutol ◽  
Darby Ball ◽  
...  

<p>The biological activation and incorporation of inorganic sulfate proceeds via a process known as sulfurylation. Transfer of a sulfuryl moiety from the activated sulfate donor, 3’-phosphoadenosine-5’-phosphosulfate (PAPS), to hydroxy-containing substrates by human phenol sulfotransferases (SULT1 family) alters substrate solubility and charge to affect the metabolism of endogenous metabolites, xenobiotics, and drugs. Current methods to monitor SULT1 activity in living cells primarily rely on radiolabeling and/or cell extractions, but these methods do not provide a direct readout of enzyme activity with a dynamic, temporally resolved spatial map in live, intact cells. To fill this gap, here, we present the development, computational modeling, <i>in vitro</i> enzymology, and biological application of Sulfotransferase Sensor-3, STS-3, an activity-based fluorescent sensor for SULT1A1, the most widely expressed and promiscuous SULT1 isoform. </p>


2020 ◽  
Author(s):  
Regina A. Baglia ◽  
Kira Mills ◽  
Koushambi Mitra ◽  
Jasmine Tutol ◽  
Darby Ball ◽  
...  

<p>The biological activation and incorporation of inorganic sulfate proceeds via a process known as sulfurylation. Transfer of a sulfuryl moiety from the activated sulfate donor, 3’-phosphoadenosine-5’-phosphosulfate (PAPS), to hydroxy-containing substrates by human phenol sulfotransferases (SULT1 family) alters substrate solubility and charge to affect the metabolism of endogenous metabolites, xenobiotics, and drugs. Current methods to monitor SULT1 activity in living cells primarily rely on radiolabeling and/or cell extractions, but these methods do not provide a direct readout of enzyme activity with a dynamic, temporally resolved spatial map in live, intact cells. To fill this gap, here, we present the development, computational modeling, <i>in vitro</i> enzymology, and biological application of Sulfotransferase Sensor-3, STS-3, an activity-based fluorescent sensor for SULT1A1, the most widely expressed and promiscuous SULT1 isoform. </p>


2014 ◽  
Vol 50 (43) ◽  
pp. 5793-5795 ◽  
Author(s):  
Lalit N. Goswami ◽  
Aslam A. Khan ◽  
Satish S. Jalisatgi ◽  
M. Frederick Hawthorne

The design, synthesis and in vitro assessment of a closo-borane based bifunctional imaging probe for dual fluorine (19F) magnetic resonance spectroscopy (19F-MRS) and fluorescence detection is reported.


Molecules ◽  
2019 ◽  
Vol 24 (13) ◽  
pp. 2394
Author(s):  
Liying Zhang ◽  
Zhiwei Yan ◽  
Youde Wang ◽  
Chengjun Song ◽  
Guangxin Miao

To explore the molecular mechanisms of BAY R3401, four types of novel photoaffinity probes bearing different secondary tags were synthesized. Their potency for glycogenolysis was evaluated in primary human liver HL-7702 cells and HepG2 cells. Probe 2d showed the best activity in primary human liver HL-7702 cells and HepG2 cells, with IC50 values of 4.45 μM and 28.49 μM, respectively. Likewise, probe 5d showed IC50 values of 6.46 μM in primary human liver HL-7702 cells and 15.29 μM in HepG2 cells, respectively. Photoaffinity labeling experiments were also performed and protein bands larger than 170 kDa were specifically tagged by probe 2d. The results suggest that the synthesized probe 2d might be a very promising tool for the isolation of the target proteins of BAY R3401.


Chirality ◽  
2018 ◽  
Vol 31 (2) ◽  
pp. 97-109 ◽  
Author(s):  
Ildikó Móczár ◽  
Péter Huszthy

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