scholarly journals Bright Chromenylium Polymethine Dyes Enable Fast, Four-Color In Vivo Imaging with Shortwave Infrared Detection

Author(s):  
Emily D. Cosco ◽  
Bernardo A. Arús ◽  
Anthony L. Spearman ◽  
Timothy L. Atallah ◽  
Irene Lim ◽  
...  

Nano Letters ◽  
2017 ◽  
Vol 17 (10) ◽  
pp. 6330-6334 ◽  
Author(s):  
Yue Chen ◽  
Daniel M. Montana ◽  
He Wei ◽  
Jose M. Cordero ◽  
Marc Schneider ◽  
...  


Biomaterials ◽  
2016 ◽  
Vol 103 ◽  
pp. 256-264 ◽  
Author(s):  
Shaoqing Feng ◽  
Jun Chen ◽  
Yan Wo ◽  
Yunxia Li ◽  
Shiyi Chen ◽  
...  


2020 ◽  
Vol 12 (12) ◽  
pp. 1123-1130
Author(s):  
Emily D. Cosco ◽  
Anthony L. Spearman ◽  
Shyam Ramakrishnan ◽  
Jakob G. P. Lingg ◽  
Mara Saccomano ◽  
...  


Nanoscale ◽  
2019 ◽  
Vol 11 (42) ◽  
pp. 19736-19741 ◽  
Author(s):  
Heng Xu ◽  
Jun Chen ◽  
Zhujun Feng ◽  
Kan Fu ◽  
Yusen Qiao ◽  
...  

A novel nerve specific imaging agent based on SWIR QD-based in vivo imaging can markedly minimize the risk of iatrogenic nerve injuries during surgeries by providing real-time and long-time SWIR images of peripheral nerves in specific.



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 ◽  
...  


2016 ◽  
Vol 54 (12) ◽  
pp. 1343-1404
Author(s):  
A Ghallab ◽  
R Reif ◽  
R Hassan ◽  
AS Seddek ◽  
JG Hengstler


2020 ◽  
Author(s):  
J Iking ◽  
S Hermann ◽  
L Honold ◽  
M Kuhlmann ◽  
M Schäfers ◽  
...  


2016 ◽  
Author(s):  
Alysha Bhatti ◽  
Almeida Gilberto Serrano de ◽  
Serena Tommasini Ghelfi ◽  
Alwyn Dart ◽  
Anabel Varela-Carver ◽  
...  




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