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Integrated Experimental and Theoretical Studies on an Electrochemical Immunosensor.

ABSTRACT: Electrochemical immunosensors (EIs) integrate biorecognition molecules (e.g., antibodies) with redox enzymes (e.g., horseradish peroxidase) to combine the advantages of immunoassays (high sensitivity and selectivity) with those of electrochemical biosensors (quantitative electrical signal). However, the complex network of mass-transfer, catalysis, and electrochemical reaction steps that produce the electrical signal makes the design and optimization of EI systems challenging. This paper presents an integrated experimental and modeling framework to address this challenge. The framework includes (1) a mechanistic mathematical model that describes the rate of key mass-transfer and reaction steps; (2) a statistical-design-of-experiments study to optimize operating conditions and validate the mechanistic model; and (3) a novel dimensional analysis to assess the degree to which individual mass-transfer and reaction steps limit the EI's signal amplitude and sensitivity. The validated mechanistic model was able to predict the effect of four independent variables (working electrode overpotential, pH, and concentrations of catechol and hydrogen peroxide) on the EI's signal magnitude. The model was then used to calculate dimensionless groups, including Damkohler numbers, novel current-control coefficients, and sensitivity-control coefficients that indicated the extent to which the individual mass-transfer or reaction steps limited the EI's signal amplitude and sensitivity.

SUBMITTER: Rafat N

PROVIDER: S-EPMC7603011 | biostudies-literature | 2020 Oct

REPOSITORIES: biostudies-literature

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Integrated Experimental and Theoretical Studies on an Electrochemical Immunosensor.

Rafat Neda N Satoh Paul P Calabrese Barton Scott S Worden Robert Mark RM

Biosensors 20201017 10

Electrochemical immunosensors (EIs) integrate biorecognition molecules (e.g., antibodies) with redox enzymes (e.g., horseradish peroxidase) to combine the advantages of immunoassays (high sensitivity and selectivity) with those of electrochemical biosensors (quantitative electrical signal). However, the complex network of mass-transfer, catalysis, and electrochemical reaction steps that produce the electrical signal makes the design and optimization of EI systems challenging. This paper presents ...[more]

PMID: 33080847

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Project description:G protein coupled receptors (GPCRs), also called 7TM receptors, form a huge superfamily of membrane proteins that, upon activation by extracellular agonists, pass the signal to the cell interior. Ligands can bind either to extracellular N-terminus and loops (e.g. glutamate receptors) or to the binding site within transmembrane helices (Rhodopsin-like family). They are all activated by agonists although a spontaneous auto-activation of an empty receptor can also be observed. Biochemical and crystallographic methods together with molecular dynamics simulations and other theoretical techniques provided models of the receptor activation based on the action of so-called "molecular switches" buried in the receptor structure. They are changed by agonists but also by inverse agonists evoking an ensemble of activation states leading toward different activation pathways. Switches discovered so far include the ionic lock switch, the 3-7 lock switch, the tyrosine toggle switch linked with the nPxxy motif in TM7, and the transmission switch. The latter one was proposed instead of the tryptophan rotamer toggle switch because no change of the rotamer was observed in structures of activated receptors. The global toggle switch suggested earlier consisting of a vertical rigid motion of TM6, seems also to be implausible based on the recent crystal structures of GPCRs with agonists. Theoretical and experimental methods (crystallography, NMR, specific spectroscopic methods like FRET/BRET but also single-molecule-force-spectroscopy) are currently used to study the effect of ligands on the receptor structure, location of stable structural segments/domains of GPCRs, and to answer the still open question on how ligands are binding: either via ensemble of conformational receptor states or rather via induced fit mechanisms. On the other hand the structural investigations of homoand heterodimers and higher oligomers revealed the mechanism of allosteric signal transmission and receptor activation that could lead to design highly effective and selective allosteric or ago-allosteric drugs.

Dataset Information

Integrated Experimental and Theoretical Studies on an Electrochemical Immunosensor.

Publications

Integrated Experimental and Theoretical Studies on an Electrochemical Immunosensor.

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