scholarly journals Site selective reading of epigenetic markers by a dual-mode synthetic receptor array

2017 ◽  
Vol 8 (5) ◽  
pp. 3960-3970 ◽  
Author(s):  
Yang Liu ◽  
Lizeth Perez ◽  
Magi Mettry ◽  
Adam D. Gill ◽  
Samantha R. Byers ◽  
...  

Arrayed, self-folding deep cavitands form a fluorescence displacement assay system for the site-selective sensing of post-translationally modified (PTM) histone peptides.

Polymers ◽  
2021 ◽  
Vol 13 (13) ◽  
pp. 2221
Author(s):  
Joseph W Lowdon ◽  
Hanne Diliën ◽  
Bart van Grinsven ◽  
Kasper Eersels ◽  
Thomas J. Cleij

The scope of the presented research orientates itself towards the development of a Molecularly Imprinted Polymer (MIP)-based dye displacement assay for the colorimetric detection of the antibiotic amoxicillin in aqueous medium. With this in mind, the initial development of an MIP capable of such a task sets focus on monolithic bulk polymerization to assess monomer/crosslinker combinations that have potential towards the binding of amoxicillin. The best performing composition (based on specificity and binding capacity) is utilized in the synthesis of MIP particles by emulsion polymerization, yielding particles that prove to be more homogenous in size and morphology compared to that of the crushed monolithic MIP, which is an essential trait when it comes to the accuracy of the resulting assay. The specificity and selectivity of the emulsion MIP proceeds to be highlighted, demonstrating a higher affinity towards amoxicillin compared to other compounds of the aminopenicillin class (ampicillin and cloxacillin). Conversion of the polymeric receptor is then undertaken, identifying a suitable dye for the displacement assay by means of binding experiments with malachite green, crystal violet, and mordant orange. Once identified, the optimal dye is then loaded onto the synthetic receptor, and the displaceability of the dye deduced by means of a dose response experiment. Alongside the sensitivity, the selectivity of the assay is scrutinized against cloxacillin and ampicillin. Yielding a dye displacement assay that can be used (semi-)quantitatively in a rapid manner.


2006 ◽  
Vol 128 (18) ◽  
pp. 6024-6025 ◽  
Author(s):  
Vadakkancheril S. Jisha ◽  
Kalliat T. Arun ◽  
Mahesh Hariharan ◽  
Danaboyina Ramaiah

2014 ◽  
Vol 50 (72) ◽  
pp. 10499-10501 ◽  
Author(s):  
Adam J. Plaunt ◽  
Kasey J. Clear ◽  
Bradley D. Smith

A 19F NMR indicator displacement assay detects phosphorylated analytes with amplified signal intensity.


Molecules ◽  
2020 ◽  
Vol 25 (22) ◽  
pp. 5222
Author(s):  
Joseph W. Lowdon ◽  
Kasper Eersels ◽  
Rocio Arreguin-Campos ◽  
Manlio Caldara ◽  
Benjamin Heidt ◽  
...  

The rapid sensing of drug compounds has traditionally relied on antibodies, enzymes and electrochemical reactions. These technologies can frequently produce false positives/negatives and require specific conditions to operate. Akin to antibodies, molecularly imprinted polymers (MIPs) are a more robust synthetic alternative with the ability to bind a target molecule with an affinity comparable to that of its natural counterparts. With this in mind, the research presented in this article introduces a facile MIP-based dye displacement assay for the detection of (±) amphetamine in urine. The selective nature of MIPs coupled with a displaceable dye enables the resulting low-cost assay to rapidly produce a clear visual confirmation of a target’s presence, offering huge commercial potential. The following manuscript characterizes the proposed assay, drawing attention to various facets of the sensor design and optimization. To this end, synthesis of a MIP tailored towards amphetamine is described, scrutinizing the composition and selectivity (ibuprofen, naproxen, 2-methoxphenidine, quetiapine) of the reported synthetic receptor. Dye selection for the development of the displacement assay follows, proceeded by optimization of the displacement process by investigating the time taken and the amount of MIP powder required for optimum displacement. An optimized dose–response curve is then presented, introducing (±) amphetamine hydrochloride (0.01–1 mg mL−1) to the engineered sensor and determining the limit of detection (LoD). The research culminates in the assay being used for the analysis of spiked urine samples (amphetamine, ibuprofen, naproxen, 2-methoxphenidine, quetiapine, bupropion, pheniramine, bromopheniramine) and evaluating its potential as a low-cost, rapid and selective method of analysis.


2018 ◽  
Vol 54 (93) ◽  
pp. 13147-13150 ◽  
Author(s):  
Yang Liu ◽  
Yaokai Duan ◽  
Adam D. Gill ◽  
Lizeth Perez ◽  
Qiaoshi Jiang ◽  
...  

A synergistic combination of a deep cavitand host, fluorophore guests and transition metal ions can be used to sense small molecule thiols of biological interest with good efficiency and selectivity in complex aqueous media.


1993 ◽  
Vol 70 (03) ◽  
pp. 448-453 ◽  
Author(s):  
Ole Nordfang ◽  
Hanne I Kristensen ◽  
Sanne Valentin ◽  
Per Østergaard ◽  
Johnny Wadt

SummaryThe anticoagulant activities of Tissue Factor Pathway Inhibitor (TFPI), heparin and hirudin were compared in intrinsic (APTT) and extrinsic (PT) activated clotting assays. In contrast to the thrombin inhibitor hirudin, heparin was 10 fold more potent in the APTT assay than in the PT assay, indicating that inhibition of intrinsic activation is important for the anticoagulant activity of heparin as measured in an APTT assay. TFPI was most potent in the PT assay and the effect of TFPI was most pronounced in the presence of other anticoagulants (heparin and hirudin). The activities of the two natural anticoagulants antithrombin III (ATIII) and TFPI were compared in a PT assay with very dilute tissue factor. In this assay system TFPI in normal plasma affected the clotting time more than ATIII in the plasma. However, when heparin was added ATIII was the major anticoagulant, but profound Prolongation of the clotting time was only seen when TFPI was also added. In an ATIII deficient plasma heparin did not augment the effect of TFPI, showing that the increased effect of TFPI in the presence of heparin is dependent on the anticoagulant activity of ATIII/heparin. The effect of TFPI at prolonged clotting times was also illustrated by the significant effect of blocking TFPI in the plasma from warfarin-treated patients. Thus TFPI is a major anticoagulant in normal plasma and the effect of TFPI is especially seen at prolonged clotting times.


1977 ◽  
Vol 37 (01) ◽  
pp. 154-161 ◽  
Author(s):  
B. A Janik ◽  
S. E Papaioannou

SummaryUrokinase, streptokinase, Brinase, trypsin, and SN 687, a bacterial exoprotease, have been evaluated in an ex vivo assay system. These enzymes were injected into rabbits and the fibrinolytic activity as well as other coagulation parameters were measured by in vitro techniques. Dose-response correlations have been made using the euglobulin lysis time as a measure of fibrinolytic activity and the 50% effective dose has been determined for each enzyme. Loading doses, equal to four times the 50% effective dose, were administered to monitor potential toxicity revealing that Brinase, trypsin, and SN 687 were very toxic at this concentration.Having established the 50% effective dose for each enzyme, further testing was conducted where relevant fibrinolytic and coagulation parameters were measured for up to two days following a 50% effective dose bolus injection of each enzyme. Our results have demonstrated that urokinase and streptokinase are plasminogen activators specifically activating the rabbit fibrinolytic system while Brinase, trypsin and SN 687 increase the general proteolytic activity in vivo.The advantages of this ex vivo assay system for evaluating relative fibrinolytic potencies and side effects for plasminogen activators and fibrinolytic proteases have been discussed.


1970 ◽  
Vol 23 (02) ◽  
pp. 191-201 ◽  
Author(s):  
H. D Bruhn ◽  
L Müller ◽  
F Duckert

SummaryA modification of the caseinolytic assay for plasminogen is described. This assay system is characterized by the following features :1. Urokinase is used as activator achieving a complete activation of the plasminogen whereas with streptokinase caseinolytically inactive plasminogen-activator complexes are formed.2. All incubation times are reduced to the minimum which is still compatible with accuracy.3. Results are expressed in percent of a standard of ten normal plasmas.4. In this two-stage assay-system (activation of plasminogen to plasmin, digestion of casein by plasmin) both stages proceed simultaneously in the same system, thus the plasmin formed is stabilized “in statu nascendi” by the casein.5. Several conditions (stability of plasminogen in frozen plasma, use of anticoagulants, reproducibility) are defined.


Sign in / Sign up

Export Citation Format

Share Document