In vivo imaging of cancer biomarkers using activatable molecular probes

2008 ◽  
Vol 4 (6) ◽  
pp. 287-305 ◽  
Author(s):  
Drew R. Elias ◽  
Daniel L.J. Thorek ◽  
Antony K. Chen ◽  
Julie Czupryna ◽  
Andrew Tsourkas
2009 ◽  
Vol 5 (11) ◽  
pp. 1279 ◽  
Author(s):  
Raphael Alford ◽  
Mikako Ogawa ◽  
Peter L. Choyke ◽  
Hisataka Kobayashi

Author(s):  
Yuqi Wang ◽  
Jianhui Weng ◽  
Xidan Wen ◽  
Yuxuan Hu ◽  
Deju Ye

Stimuli-responsive in situ self-assembly of small molecule probes into nanostructures has been promising for the construction of molecular probes for in vivo imaging.


2012 ◽  
Vol 1 (1) ◽  
pp. 55-62 ◽  
Author(s):  
Soyoun Kim ◽  
Kiweon Cha ◽  
In-San Kim

2020 ◽  
Vol 11 (1) ◽  
pp. 224-231 ◽  
Author(s):  
Eman A. Akam ◽  
Eric Abston ◽  
Nicholas J. Rotile ◽  
Hannah R. Slattery ◽  
Iris Y. Zhou ◽  
...  

Improving the aldehyde-reactivity of hydrazine molecular probes translates to increased on-target accumulation in fibrotic lungs and superior visualization of disease.


2009 ◽  
Vol 97 (9) ◽  
pp. L22-L24 ◽  
Author(s):  
Mikhail Y. Berezin ◽  
Walter J. Akers ◽  
Kevin Guo ◽  
Georg M. Fischer ◽  
Ewald Daltrozzo ◽  
...  

Research ◽  
2020 ◽  
Vol 2020 ◽  
pp. 1-13
Author(s):  
Yuxuan Hu ◽  
Yuqi Wang ◽  
Xidan Wen ◽  
Yifan Pan ◽  
Xiaoyang Cheng ◽  
...  

Noninvasive in vivo imaging of hepatic glutathione (GSH) levels is essential to early diagnosis and prognosis of acute hepatitis. Although GSH-responsive fluorescence imaging probes have been reported for evaluation of hepatitis conditions, the low penetration depth of light in liver tissue has impeded reliable GSH visualization in the human liver. We present a liver-targeted and GSH-responsive trimodal probe (GdNPs-Gal) for rapid evaluation of lipopolysaccharide- (LPS-) induced acute liver inflammation via noninvasive, real-time in vivo imaging of hepatic GSH depletion. GdNPs-Gal are formed by molecular coassembly of a GSH-responsive Gd(III)-based MRI probe (1-Gd) and a liver-targeted probe (1-Gal) at a mole ratio of 5/1 (1-Gd/1-Gal), which shows high r1 relaxivity with low fluorescence and fluorine magnetic resonance spectroscopic (19F-MRS) signals. Upon interaction with GSH, 1-Gd and 1-Gal are cleaved and GdNPs-Gal rapidly disassemble into small molecules 2-Gd, 2-Gal, and 3, producing a substantial decline in r1 relaxivity with compensatory enhancements in fluorescence and 19F-MRS. By combining in vivo magnetic resonance imaging (1H-MRI) with ex vivo fluorescence imaging and 19F-MRS analysis, GdNPs-Gal efficiently detect hepatic GSH using three independent modalities. We noninvasively visualized LPS-induced liver inflammation and longitudinally monitored its remediation in mice after treatment with an anti-inflammatory drug, dexamethasone (DEX). Findings highlight the potential of GdNPs-Gal for in vivo imaging of liver inflammation by integrating molecular coassembly with GSH-driven disassembly, which can be applied to other responsive molecular probes for improved in vivo imaging.


Author(s):  
Xuan Zhang ◽  
Sharon Bloch ◽  
Walter Akers ◽  
Samuel Achilefu

2020 ◽  
Vol 48 (6) ◽  
pp. 2657-2667
Author(s):  
Felipe Montecinos-Franjola ◽  
John Y. Lin ◽  
Erik A. Rodriguez

Noninvasive fluorescent imaging requires far-red and near-infrared fluorescent proteins for deeper imaging. Near-infrared light penetrates biological tissue with blood vessels due to low absorbance, scattering, and reflection of light and has a greater signal-to-noise due to less autofluorescence. Far-red and near-infrared fluorescent proteins absorb light >600 nm to expand the color palette for imaging multiple biosensors and noninvasive in vivo imaging. The ideal fluorescent proteins are bright, photobleach minimally, express well in the desired cells, do not oligomerize, and generate or incorporate exogenous fluorophores efficiently. Coral-derived red fluorescent proteins require oxygen for fluorophore formation and release two hydrogen peroxide molecules. New fluorescent proteins based on phytochrome and phycobiliproteins use biliverdin IXα as fluorophores, do not require oxygen for maturation to image anaerobic organisms and tumor core, and do not generate hydrogen peroxide. The small Ultra-Red Fluorescent Protein (smURFP) was evolved from a cyanobacterial phycobiliprotein to covalently attach biliverdin as an exogenous fluorophore. The small Ultra-Red Fluorescent Protein is biophysically as bright as the enhanced green fluorescent protein, is exceptionally photostable, used for biosensor development, and visible in living mice. Novel applications of smURFP include in vitro protein diagnostics with attomolar (10−18 M) sensitivity, encapsulation in viral particles, and fluorescent protein nanoparticles. However, the availability of biliverdin limits the fluorescence of biliverdin-attaching fluorescent proteins; hence, extra biliverdin is needed to enhance brightness. New methods for improved biliverdin bioavailability are necessary to develop improved bright far-red and near-infrared fluorescent proteins for noninvasive imaging in vivo.


2005 ◽  
Vol 25 (1_suppl) ◽  
pp. S588-S588
Author(s):  
Vladimir Kepe ◽  
Gregory M Cole ◽  
Jie Liu ◽  
Dorothy G Flood ◽  
Stephen P Trusko ◽  
...  

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