A Bimodal, Cationic, and Water-Soluble Calix[4]arene Conjugate: Design, Synthesis, Characterization, and Transfection of Red Fluorescent Protein Encoded Plasmid in Cancer Cells

2017 ◽  
Vol 9 (6) ◽  
pp. 5109-5117 ◽  
Author(s):  
Kushal Samanta ◽  
Dnyanesh S. Ranade ◽  
Aekta Upadhyay ◽  
Prasad P. Kulkarni ◽  
Chebrolu Pulla Rao
Keyword(s):  
Cancer Cells ◽  
Fluorescent Protein ◽  
Water Soluble ◽  
Red Fluorescent Protein ◽  
Design Synthesis

scholarly journals Fluorescently Tagged CCL19 and CCL21 to Monitor CCR7 and ACKR4 Functions

2018 ◽  
Vol 19 (12) ◽  
pp. 3876 ◽  
Author(s):  
Vladimir Purvanov ◽  
Christoph Matti ◽  
Guerric P. B. Samson ◽  
Ilona Kindinger ◽  
Daniel F. Legler
Keyword(s):  
Cancer Cells ◽  
Chemokine Receptors ◽  
Fluorescent Protein ◽  
Adaptive Immune Response ◽  
Cell Types ◽  
Red Fluorescent Protein ◽  
Adaptive Immune ◽  
Guidance Cues ◽  
Cell Locomotion ◽  
Health And Disease

Chemokines are essential guidance cues orchestrating cell migration in health and disease. Cognate chemokine receptors sense chemokine gradients over short distances to coordinate directional cell locomotion. The chemokines CCL19 and CCL21 are essential for recruiting CCR7-expressing dendritic cells bearing pathogen-derived antigens and lymphocytes to lymph nodes, where the two cell types meet to launch an adaptive immune response against the invading pathogen. CCR7-expressing cancer cells are also recruited by CCL19 and CCL21 to metastasize in lymphoid organs. In contrast, atypical chemokine receptors (ACKRs) do not transmit signals required for cell locomotion but scavenge chemokines. ACKR4 is crucial for internalizing and degrading CCL19 and CCL21 to establish local gradients, which are sensed by CCR7-expressing cells. Here, we describe the production of fluorescently tagged chemokines by fusing CCL19 and CCL21 to monomeric red fluorescent protein (mRFP). We show that purified CCL19-mRFP and CCL21-mRFP are versatile and powerful tools to study CCR7 and ACKR4 functions, such as receptor trafficking and chemokine scavenging, in a spatiotemporal fashion. We demonstrate that fluorescently tagged CCL19 and CCL21 permit the visualization and quantification of chemokine gradients in real time, while CCR7-expressing leukocytes and cancer cells sense the guidance cues and migrate along the chemokine gradients.

scholarly journals Electrodelivery of Drugs into Cancer Cells in the Presence of Poloxamer 188

2010 ◽  
Vol 2010 ◽  
pp. 1-11 ◽  
Author(s):  
Iana Tsoneva ◽  
Iordan Iordanov ◽  
Annette J. Berger ◽  
Toma Tomov ◽  
Biliana Nikolova ◽  
...  
Keyword(s):  
Small Molecules ◽  
Cancer Cells ◽  
Nude Mice ◽  
Propidium Iodide ◽  
Hela Cells ◽  
Fluorescent Protein ◽  
Electrical Pulse ◽  
Red Fluorescent Protein ◽  
Poloxamer 188 ◽  
Pore Structures

In the present study it is shown that poloxamer 188, added before or immediately after an electrical pulse used for electroporation, decreases the number of dead cells and at the same time does not reduce the number of reversible electropores through which small molecules (cisplatin, bleomycin, or propidium iodide) can pass/diffuse. It was suggested that hydrophobic sections of poloxamer 188 molecules are incorporated into the edges of pores and that their hydrophilic parts act as brushy pore structures. The formation of brushy pores may reduce the expansion of pores and delay the irreversible electropermeability. Tumors were implanted subcutaneously in both flanks of nude mice using HeLa cells, transfected with genes for red fluorescent protein and luciferase. The volume of tumors stopped to grow after electrochemotherapy and the use of poloxamer 188 reduced the edema near the electrode and around the subcutaneously growing tumors.

scholarly journals Design, synthesis and cytotoxic activity of water-soluble quinones with dibromo-p-benzoquinone cores and amino oligo(ethylene glycol) side chains against MCF-7 breast cancer cells

MedChemComm ◽  
2017 ◽  
Vol 8 (3) ◽  
pp. 662-672 ◽  
Author(s):  
Leon F. Scherz ◽  
Engy A. Abdel-Rahman ◽  
Sameh S. Ali ◽  
A. Dieter Schlüter ◽  
Mona A. Abdel-Rahman
Keyword(s):  
Breast Cancer ◽  
Ethylene Glycol ◽  
Cancer Cells ◽  
Breast Cancer Cells ◽  
Water Soluble ◽  
Fibroblast Cells ◽  
Design Synthesis ◽  
Human Fibroblast Cells ◽  
Mcf 7

Novel water-soluble dibromo-p-benzoquinones were synthesized and their in vitro cytotoxicity against MCF-7 breast cancer cells and human fibroblast cells was evaluated.

Water-soluble amphiphilic ruthenium(ii) polypyridyl complexes as potential light-activated therapeutic agents

2020 ◽  
Vol 56 (65) ◽  
pp. 9332-9335
Author(s):  
Sandra Estalayo-Adrián ◽  
Salvador Blasco ◽  
Sandra A. Bright ◽  
Gavin J. McManus ◽  
Guillermo Orellana ◽  
...  
Keyword(s):  
Cervical Cancer ◽  
Cancer Cells ◽  
Cellular Uptake ◽  
Therapeutic Agents ◽  
Water Soluble ◽  
Polypyridyl Complexes ◽  
Cervical Cancer Cells

Two new water-soluble amphiphilic Ru(ii) polypyridyl complexes were synthesised and their photophysical and photobiological properties evaluated; both complexes showed a rapid cellular uptake and phototoxicity against HeLa cervical cancer cells.

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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