A novel, sensitive electrochemical immunoassay has been developed using a colloidal gold label that, after oxidative gold metal dissolution in an acidic solution, was indirectly determined by anodic stripping voltammetry (ASV) at a single-use carbon-based screen-printed electrode (SPE). The use of disposable electrodes allows for simplified measurement in 35 microL of solution. The method was evaluated for a noncompetitive heterogeneous immunoassay of an immunoglobulin G (IgG) and a concentration as low as 3 x 10(-12) M was determined, which is competitive with colorimetric ELISA or with immunoassays based on fluorescent europium chelate labels. The high performance of the method is related to the sensitive ASV determination of gold(III) at a SPE (detection limit of 5 x 10(-9) M) and to the release of a large number of gold(III) ions from each gold particle anchored on the immunocomplex (e.g., 1.7 x 10(5) gold atoms are theoretically contained in a 18-nm spherical gold particle).
The electrochemical reduction of phenylazide or phenylacetylene diazonium salts leads to the grafting of azido or ethynyl groups onto the surface of carbon electrodes. In the presence of copper(I) catalyst, these azide- or alkyne-modified surfaces react efficiently and rapidly with compounds bearing an acetylene or azide function, thus forming a covalent 1,2,3-triazole linkage by means of click chemistry. This was illustrated with the surface coupling of ferrocenes functionalized with an ethynyl or azido group and the biomolecule biotin terminated by an acetylene group.
Ongoing developments of sustainable energy technologies based on high-surface-area semiconductive metal oxide electrodes operating under mild and safe aqueous conditions require deep understanding of proton and electron transfer/transport throughout their porous structure. To address this issue, we investigated the electrochemical reductive protonation of high surface area nanostructured amorphous TiO 2 electrodes (produced by glancing angle deposition) in both buffered and unbuffered aqueous solutions. Quantitative analysis of the two charge storage mechanisms was achieved, allowing proper deconvolution of the electrical double-layer capacitive charge storage from the reversible faradaic one resulting from the proton-coupled reduction of bulk TiO 2. We evidence that this latter process occurs reversibly and extensively (up to an intercalation ratio of 20%) not only under strongly acidic pH conditions but also, more interestingly, under neutral pH with the intercalated proton arising from the buffer rather than water. Moreover, we show that in comparison with reductive Li + intercalation the proton-coupled electron charge storage occurs more rapidly (in a few seconds). This important finding suggests that a high-rate and high-power charge storage device could potentially be achieved with the reversible H +-coupled charge/discharge process in TiO 2 at neutral pH, opening thus new opportunities to the development of eco-friendly batteries for electrical energy storage.
Rechargeable batteries based on MnO2 cathodes, able to operate in mild aqueous electrolytes, have attracted attention due to their appealing features for the design of low‐cost stationary energy storage devices. However, the charge/discharge mechanism of MnO2 in such media is still a matter of debate. Here, an in‐depth quantitative spectroelectrochemical analysis of MnO2 thin‐films provides a set of unrivaled mechanistic insights. A major finding is that charge storage occurs through the reversible two‐electron faradaic conversion of MnO2 into Mn2+ in the presence of a wide range of weak Brønsted acids, including the [Zn(H2O)6]2+ or [Mn(H2O)6]2+ complexes present in aqueous Zn/MnO2 batteries. Furthermore, it is shown that buffered electrolytes loaded with Mn2+ are ideal to achieve highly reversible conversion of MnO2 with both high gravimetric capacity and remarkably stable charging/discharging potentials. In the most favorable case, a record gravimetric capacity of 450 mA·h·g−1 is obtained at a high rate of 1.6 A·g−1, with a Coulombic efficiency close to 100% and a MnO2 utilization of 84%. Overall, the present results challenge the common view on MnO2 the charge storage mechanism in mild aqueous electrolytes and underline the benefit of buffered electrolytes for high‐performance rechargeable aqueous batteries.
In this work, monolayers of metal complexes were covalently attached to the surface of carbon electrodes with the goal of binding monolayers of histidine-tagged proteins with a controlled molecular orientation and a maintained biological activity. In this novel method, which is simple, versatile, and efficient, the covalent attachment was accomplished in a single step by the electrochemical reduction of aryl diazonium ions that were substituted with a nitrilotriacetic (NTA) or an imminodiacetic (IDA) ligand at the para position. The transient aryl radicals that were generated in the reduction were grafted to the surfaces of glassy carbon, highly oriented pyrolitic graphite, and graphite-based screen-printed electrodes, producing dense monolayers of the ligands. The NTA- and IDA-modified electrodes were shown to efficiently chelate Cu(II) and Ni(II) ions. The presence of the metal was established using X-ray photoelectron spectroscopy and electrochemistry. Surface coverages of the ligands were indirectly determined from the electroactivity of the copper(II) complex formed on the electrode surface. Studies on the effect of electrodeposition time and potential showed that, at sufficiently negative potentials, the surface coverage reached a saturating value in less than 2 min of electrodeposition time, which corresponds to the formation of a close-packed monolayer of ligand on the electrode surface. Once loaded with a metal ion, the modified electrode was able to bind specifically to histidine-tagged proteins such as the horseradish peroxidase (His-HRP) or to an enhanced, recombinant green-fluorescent protein via its N-terminal hexahistidine tail. In the case of His-HRP, the amount of active enzyme specifically immobilized by metal-chelating binding was determined from the analysis of electrocatalytic currents using cyclic voltammetry. The electrochemical grafting makes it possible to accurately controlled and electronically address the amount of deposited ligand on the conductive surfaces of carbon electrodes with any size and shape.
The proof-of-principle of a nonoptical real-time PCR method based on the electrochemical monitoring of a DNA intercalating redox probe that becomes considerably less easily electrochemically detectable once intercalated to the amplified double-stranded DNA is demonstrated. This has been made possible thanks to the finding of a redox intercalator that (i) strongly and specifically binds to the amplified double-stranded DNA, (ii) does not significantly inhibit PCR, (iii) is chemically stable under PCR cycling, and (iv) is sensitively detected by square wave voltammetry during PCR cycling. Among the different DNA intercalating redox probes that we have investigated, namely, methylene blue, Os[(bpy)(2)phen](2+), Os[(bpy)(2)DPPZ](2+), Os[(4,4'-dimethyl-bpy)(2)DPPZ](2+) and Os[(4,4'-diamino-bpy)(2)DPPZ](2+) (with bpy = 2,2'-bipyridine, phen = phenanthroline, and DPPZ = dipyrido[3,2-a:2',3'-c]phenazine), the one and only compound with which it has been possible to demonstrate the proof-of-concept is the Os[(bpy)(2)DPPZ](2+). In terms of analytical performances, the methodology described here compares well with optical-based real-time PCRs, offering finally the same advantages than the popular and routinely used SYBR Green-based real-time fluorescent PCR, but with the additional incomes of being potentially much cheaper and easier to integrate in a hand-held miniaturized device.
A precise determination of the complex mechanism of catalysis and inhibition involved in the reaction of HRP with H(2)O(2) as substrate and an outersphere single electron donor ([Os(bpy)(2)pyCl](+)) as cosubstrate is made possible by a systematic analysis of the cyclic voltammetric responses as a function of the scan rate and of the substrate and cosubstrate concentrations, complemented by spectrophotometric steady-state and stopped-flow experiments. The bell-shaped calibration curve relating the electrochemical response to the concentration of H(2)O(2) is qualitatively and quantitatively explained by taking into account the conversion of the catalytically active forms of the enzyme into the inactive oxyperoxidase in addition to the primary catalytic cycle. These characteristics should be kept in mind in biosensor applications of HRP. The ensuing analysis and data allow one to predict biosensor amperometric responses in all practical cases. From a mechanistic standpoint, conditions may, however, be defined which render inhibition insignificant, thus allowing an electrochemical characterization of the primary catalytic cycle. At very low concentrations of H(2)O(2), its diffusion tends to control the electrochemical response, resulting in proportionality with H(2)O(2) concentration instead of the square root dependence characteristic of the classical catalytic currents. Intriguing hysteresis and trace crossings behaviors are also quantitatively explained in the framework of the same mechanism. As a consequence of the precise dissection of the rather complex reaction mechanism into its various elementary steps, a strategy may be devised for gaining a better understanding of the mechanism and reactivity patterns of each elementary step.
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.
hi@scite.ai
10624 S. Eastern Ave., Ste. A-614
Henderson, NV 89052, USA
Copyright © 2024 scite LLC. All rights reserved.
Made with 💙 for researchers
Part of the Research Solutions Family.