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Label-Free Electrochemical Immunosensor Based on Ionic Liquid Containing Dialdehyde As a Novel Linking Agent for the Antibody Immobilization.

ABSTRACT: Demand for label-free electrochemical immunosensor has resulted in extensive research in improving the conductivity of a sensing interface and antibody immobilization. In this paper, an electrochemical immunosensor for prostate specific antigen based on dialdehyde-functionalized ionic liquid used as a novel linking reagent to replace glutaraldehyde for the antibody immobilization is described. The novel linking reagent enhanced the conductivity of the sensing interface. Thus, the proposed immunosensor had a wider linear range of 0.05-30 ng mL-1, with a lower detection limit of 0.04 ng mL-1 compared with the immunosensor based on glutaraldehyde for the antibody immobilization.

SUBMITTER: Shen Y

PROVIDER: S-EPMC6173497 | biostudies-literature | 2018 Sep

REPOSITORIES: biostudies-literature

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Label-Free Electrochemical Immunosensor Based on Ionic Liquid Containing Dialdehyde As a Novel Linking Agent for the Antibody Immobilization.

Shen Youming Y Shen Guangyu G Zhang Youyu Y

ACS omega 20180914 9

Demand for label-free electrochemical immunosensor has resulted in extensive research in improving the conductivity of a sensing interface and antibody immobilization. In this paper, an electrochemical immunosensor for prostate specific antigen based on dialdehyde-functionalized ionic liquid used as a novel linking reagent to replace glutaraldehyde for the antibody immobilization is described. The novel linking reagent enhanced the conductivity of the sensing interface. Thus, the proposed immuno ...[more]

PMID: 30320258

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Project description:The formation of ionic liquid (IL) mixtures has been proposed as an approach to rationally fine-tune the physicochemical properties of ILs for a variety of applications. However, the effects of forming such mixtures on the resultant properties of the liquids are only beginning to be understood. Towards a more complete understanding of both the thermodynamics of mixing ILs and the effect of mixing these liquids on their structures and physicochemical properties, the spatial arrangement and free volume of IL mixtures containing the common [C4C1im]+ cation and different anions have been systematically explored using small angle X-ray scattering (SAXS), positron annihilation lifetime spectroscopy (PALS) and 129Xe NMR techniques. Anion size has the greatest effect on the spatial arrangement of the ILs and their mixtures in terms of the size of the non-polar domains and inter-ion distances. It was found that differences in coulombic attraction between oppositely charged ions arising from the distribution of charge density amongst the atoms of the anion also significantly influences these inter-ion distances. PALS and 129Xe NMR results pertaining to the free volume of these mixtures were found to strongly correlate with each other despite the vastly different timescales of these techniques. Furthermore, the excess free volumes calculated from each of these measurements were in excellent agreement with the excess volumes of mixing measured for the IL mixtures investigated. The correspondence of these techniques indicates that the static and dynamic free volume of these liquid mixtures are strongly linked. Consequently, fluxional processes such as hydrogen bonding do not significantly contribute to the free volumes of these liquids compared to the spatial arrangement of ions arising from their size, shape and coulombic attraction. Given the relationship between free volume and transport properties such as viscosity and conductivity, these results provide a link between the structures of IL mixtures, the thermodynamics of mixing and their physicochemical properties.

Dataset Information

Label-Free Electrochemical Immunosensor Based on Ionic Liquid Containing Dialdehyde As a Novel Linking Agent for the Antibody Immobilization.

Publications

Label-Free Electrochemical Immunosensor Based on Ionic Liquid Containing Dialdehyde As a Novel Linking Agent for the Antibody Immobilization.

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