A Colorimetric and “Turn-On” Fluorescent Chemosensor for Metal Ion Based on Rhodamine Derivative

2014 ◽  
Vol 955-959 ◽  
pp. 267-270
Author(s):  
Hao Zhang ◽  
Xi Jiang

The recognition and sensing of biologically and environmentally important species has emerged as a significant goal in the field of chemical sensors in recent years1. Fluorogenic methods in conjunction with suitable probes are preferable approaches for the measurement of these analytes because fluorimetry is rapidly performed, is nondestructive, is highly sensitive, is suitable for high-throughput screening applications2,3. We synthesized rhodamine derivatives compounds by a Schiff base reaction.

RSC Advances ◽  
2015 ◽  
Vol 5 (81) ◽  
pp. 65731-65738 ◽  
Author(s):  
Divya Singhal ◽  
Neha Gupta ◽  
Ashok Kumar Singh

2-((3-Methylthiophen-2-yl)methyleneamino)benzenethiol (Probe 1) is selective for Hg2+. The binding affinity of Hg2+ with Probe 1 was confirmed by DFT and electrochemical behaviour. The limit of detection was 20 μM with 2 : 1 stoichiometry of 1 + Hg2+ complex.


2003 ◽  
pp. 289-316
Author(s):  
Jaime C. Grunlan ◽  
Dennis Saunders ◽  
Jay Akhave ◽  
Mark Licon ◽  
Marcel Murga ◽  
...  

2014 ◽  
Vol 5 (10) ◽  
pp. 4012-4016 ◽  
Author(s):  
Pengwei Jin ◽  
Changhong Jiao ◽  
Zhiqian Guo ◽  
Ye He ◽  
Shiqin Zhu ◽  
...  

A rational design of turn-on fluorescent chemosensors for monitoring α-ketoglutaric acid has been developed with a microfluidic chip, indicative of a potential platform for high-throughput screening and monitoring of kinetics, especially in biological fields.


2006 ◽  
Vol 11 (4) ◽  
pp. 413-422 ◽  
Author(s):  
Casey Stankewicz ◽  
Frauke H. Rininsland

Aberrant regulation of phosphoinositide 3-kinase (PI3K) activity is implicated in various diseases such as cancer and diabetes. Thus, high-throughput screening (HTS) of small-molecule inhibitors for PI3 kinases is an appealing strategy for drug development. Despite the attractiveness of lipid kinases as drug targets, screening for inhibitors for PI3K activities has been hampered by limited assay formats adaptable for HTS. The authors describe a homogeneous, direct, and nonradioactive assay for highly sensitive detection of PI3Kα, β, δ, and γ activities, which is suitable for HTS. The assay is based on fluorescence superquenching of a conjugated polymer upon metal-ion-mediated association of phosphorylated and dye-labeled substrates. As a result of phosphorylation, quencher and polymer are brought into proximity, and fluorescent energy transfer occurs. This event can be monitored as either fluorescence quench of the polymer or as enhanced emission from the quencher. Ratiometric analysis of the wavelengths eliminates interferences from autofluorescing compounds, which are present in HTS libraries. The platform has been adapted for the 384-well microplate format and delivers Z factors of > 0.6 at substrate conversions as low as 7%. Using this assay platform, several unreported inhibitors and activators of PI3Ks were identified in an 84- compound screen.


2006 ◽  
Vol 11 (7) ◽  
pp. 836-843 ◽  
Author(s):  
Yu-Wei Wu ◽  
Yu-Hui Tsai

Transglutaminases (TGs) are widely distributed enzymes that catalyze posttranslational modification of proteins by Ca2+-dependent cross-linking reactions. The family members of TGs participate in many significant processes of biological functions such as tissue regeneration, cell differentiation, apoptosis, and certain pathologies. A novel technique for TG activity assay was developed in this study. It was based on the rapid capturing, fluorescence quenching, and fast separation of the unreacted fluorescent molecules from the macromolecular product with magnetic dextran-coated charcoal. As few as 3 ng of guinea pig liver transglutaminase (gpTG) could be detected by the method; activities of 96 TG samples could be measured within an hour. The Km of gpTG determined by this method for monodansylcadaverine (dansyl-CAD) and N, N-dimethylcasein was 14 and 5 μM, respectively. A typical competitive inhibition pattern of cystamine on dansyl-CAD for gpTG activity was also demonstrated. The application of this technique is not limited to the use of dansyl-CAD as the fluorescent substrate of TG; other small fluor-labeled TG substrates may substitute dansyl-CAD. Finally, this method is rapid, highly sensitive, and inexpensive. It is suitable not only for high-throughput screening of enzymes or enzyme inhibitors but also for enzyme kinetic analysis.


2015 ◽  
Vol 44 (48) ◽  
pp. 20830-20833 ◽  
Author(s):  
Si-Quan Jiang ◽  
Zi-Yan Zhou ◽  
Shu-Ping Zhuo ◽  
Guo-Gang Shan ◽  
Ling-Bao Xing ◽  
...  

An in situ-generated iron(iii) complex with a 1,8-naphthalene-based Schiff base unit has been rationally designed, which exhibits a highly selective response and excellent sensitivity for the turn-on detection of PO43− anions.


Lab on a Chip ◽  
2021 ◽  
Author(s):  
Maximilian O. Besenhard ◽  
Dai Jiang ◽  
Quentin A. Pankhurst ◽  
Paul Southern ◽  
Spyridon Damilos ◽  
...  

A highly sensitive magnetometer for flow chemistry to characterise magnetic nanoparticles in solution, in situ and in real-time is presented. This facilitates continuous quality control and high-throughput screening of magnetic nanoparticle syntheses.


2017 ◽  
Author(s):  
Aparna Mohanakrishnan ◽  
Triet Vincent M. Tran ◽  
Meera Kumar ◽  
Hong Chen ◽  
Bruce A. Posner ◽  
...  

AbstractClathrin-mediated endocytosis is the major pathway by which cells internalize materials from the external environment. Dynamin, a large multidomain GTPase, is a key regulator of clathrin-mediated endocytosis. It assembles at the necks of invaginated clathrin-coated pits and, through GTP hydrolysis, catalyzes scission and release of clathrin-coated vesicles from the plasma membrane. Several small molecule inhibitors of dynamin’s GTPase activity, such as Dynasore and Dyngo-4a, are currently available, although their specificity has been brought into question. Previous screens for these inhibitors measured dynamin’s stimulated GTPase activity due to lack of sufficient sensitivity, hence the mechanisms by which they inhibit dynamin are uncertain. We report a highly sensitive fluorescence-based assay capable of detecting dynamin’s basal GTPase activity under conditions compatible with high throughput screening. Utilizing this optimized assay, we conducted a pilot screen of 8000 compounds and identified several “hits” that inhibit the basal GTPase activity of dynamin-1. Subsequent dose-response curves were used to validate the activity of these compounds. Interestingly, we found neither Dynasore nor Dyngo-4a inhibited dynamin’s basal GTPase activity, although both inhibit assembly-stimulated GTPase activity. This assay provides the basis for a more extensive search for robust dynamin inhibitors.


2012 ◽  
Vol 17 (7) ◽  
pp. 993-998 ◽  
Author(s):  
Kris F. Sachsenmeier ◽  
Carl Hay ◽  
Erin Brand ◽  
Lori Clarke ◽  
Kim Rosenthal ◽  
...  

5′-Ectonucleotidase (NT5E) catalyzes the conversion of adenosine monophosphate to adenosine and free phosphate. The role of this ectonucleotidase and its production of adenosine are linked with immune function, angiogenesis, and cancer. NT5E activity is typically assayed either by chromatographic quantification of substrates and products using high-performance liquid chromatography (HPLC) or by quantification of free phosphate using malachite green. These methods are not suitable for robust screening assays of NT5E activity. HPLC is not readily suitable for the rapid and efficient assay of multiple samples and malachite green is highly sensitive to the phosphate-containing buffers common in various media and sample buffers. Here the development and validation of a novel high-throughput ectonucleotidase screening assay are described, which makes use of a luciferase-based assay reagent, the Promega CellTiter-Glo kit, to measure the catabolism of AMP by NT5E. This multiwell plate-based assay facilitates the screening of potential ectonucleotidase antagonists and is unaffected by the presence of contaminating phosphate molecules present in screening samples.


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