scholarly journals Central C–C bonding increases optical and chemical stability of NIR fluorophores

RSC Advances ◽  
2014 ◽  
Vol 4 (102) ◽  
pp. 58762-58768 ◽  
Author(s):  
Hoon Hyun ◽  
Eric A. Owens ◽  
Lakshminarayana Narayana ◽  
Hideyuki Wada ◽  
Julien Gravier ◽  
...  
Keyword(s):  
Chemical Stability ◽  
Near Infrared ◽  
Recent Advances

Functional near-infrared (NIR) fluorophores have played a major role in the recent advances in bioimaging, and central C–C bonding will aid in the applicability of heptamethine cyanines in targeted in vivo imaging.

De Novo Design of Chemical Stability Near-Infrared Molecular Probes for High-Fidelity Hepatotoxicity Evaluation In Vivo

2019 ◽  
Vol 141 (15) ◽  
pp. 6352-6361 ◽  
Author(s):  
Dan Cheng ◽  
Juanjuan Peng ◽  
Yun Lv ◽  
Dongdong Su ◽  
Dongjie Liu ◽  
...  
Keyword(s):  
Chemical Stability ◽  
Near Infrared ◽  
De Novo ◽  
De Novo Design ◽  
Molecular Probes ◽  
High Fidelity

scholarly journals Recent Advances in Vascular Imaging

2020 ◽  
Vol 40 (12) ◽  
Author(s):  
Kensuke Nishimiya ◽  
Yasuharu Matsumoto ◽  
Hiroaki Shimokawa
Keyword(s):  
Optical Coherence Tomography ◽  
Intravascular Ultrasound ◽  
Near Infrared ◽  
Ex Vivo ◽  
Clinical Manifestations ◽  
Vascular Imaging ◽  
Imaging Modalities ◽  
Optical Coherence ◽  
Recent Advances

Recent advances in vascular imaging have enabled us to uncover the underlying mechanisms of vascular diseases both ex vivo and in vivo. In the past decade, efforts have been made to establish various methodologies for evaluation of atherosclerotic plaque progression and vascular inflammatory changes in addition to biomarkers and clinical manifestations. Several recent publications in Arteriosclerosis, Thrombosis, and Vascular Biology highlighted the essential roles of in vivo and ex vivo vascular imaging, including magnetic resonance image, computed tomography, positron emission tomography/scintigraphy, ultrasonography, intravascular ultrasound, and most recently, optical coherence tomography, all of which can be used in bench and clinical studies at relative ease. With new methods proposed in several landmark studies, these clinically available imaging modalities will be used in the near future. Moreover, future development of intravascular imaging modalities, such as optical coherence tomography–intravascular ultrasound, optical coherence tomography–near-infrared autofluorescence, polarized-sensitive optical coherence tomography, and micro-optical coherence tomography, are anticipated for better management of patients with cardiovascular disease. In this review article, we will overview recent advances in vascular imaging and ongoing works for future developments.

Fluorescent proteins for in vivo imaging, where's the biliverdin?

2020 ◽  
Vol 48 (6) ◽  
pp. 2657-2667
Author(s):  
Felipe Montecinos-Franjola ◽  
John Y. Lin ◽  
Erik A. Rodriguez
Keyword(s):  
Hydrogen Peroxide ◽  
In Vivo Imaging ◽  
Near Infrared ◽  
Fluorescent Protein ◽  
Fluorescent Proteins ◽  
Fluorescent Imaging ◽  
Infrared Light ◽  
Red Fluorescent Protein ◽  
Color Palette

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.

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