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Enzyme-linked immunosorbent assays (ELISA) have been widely used to detect disease-related antigens in clinical and research laboratories. One of the main drawbacks of ELISA is the utilization of physical adsorption for immobilizing antibodies on a surface, causing low sensitivity, reproducibility, and precision. In this study, we applied a BC-MAP linker composed of antibody-immobilizing BC domains of protein A and surface-adhesive mussel adhesive protein (MAP) to an ELISA platform to overcome these limitations. The performance of ELISA using BC-MAP linker was compared with that of untreated ELISA. BC-MAP proteins were reproducibly coated to the surface while exposing BC domains, resulting in twofold higher sensitivity and improved reproducibility of ELISA compared to the untreated ELISA utilizing physical adsorption of antibodies. Thus, the proposed method could be successfully used in ELISA platforms to diagnose and manage diseases. [ABSTRACT FROM AUTHOR]

Boronic acids (BAs) provide strong potential in orientation immobilization of antibody and the modification method is crucial for efficiency optimization. A highly effective method has been developed for rapid antibody immobilization on gold electrodes through the electrodeposition of a BA–containing linker in this study. Aniline-based BA forms a condense layer while antibody could automatically immobilize on the surface of the electrode. Compare to traditional self-assembled monolayer method, the electrodeposition process dramatically reduces the modification time from days to seconds. It also enhances the immobilized efficiency from 95 to 408 (ng/cm2) with a strong preference being exhibited for shorter aniline-based linkers.

Boronic acids (BAs) provide strong potential in orientation immobilization of antibody and the modification method is crucial for efficiency optimization. A highly effective method has been developed for rapid antibody immobilization on gold electrodes through the electrodeposition of a BA–containing linker in this study. Aniline-based BA forms a condense layer while antibody could automatically immobilize on the surface of the electrode. Compare to traditional self-assembled monolayer method, the electrodeposition process dramatically reduces the modification time from days to seconds. It also enhances the immobilized efficiency from 95 to 408 (ng/cm2) with a strong preference being exhibited for shorter aniline-based linkers. [ABSTRACT FROM AUTHOR]

Boronic acids (BAs) provide strong potential in orientation immobilization of antibody and the modification method is crucial for efficiency optimization. A highly effective method has been developed for rapid antibody immobilization on gold electrodes through the electrodeposition of a BA⁻containing linker in this study. Aniline-based BA forms a condense layer while antibody could automatically immobilize on the surface of the electrode. Compare to traditional self-assembled monolayer method, the electrodeposition process dramatically reduces the modification time from days to seconds. It also enhances the immobilized efficiency from 95 to 408 (ng/cm²) with a strong preference being exhibited for shorter aniline-based linkers.