Immobilized avidin–biotin complexes were used to release biotinylated (bio)molecules upon producing local pH changes near an electrode surface by electrochemical reactions. Nitro-avidin complex with biotin was dissociated by increasing local...
Regulation of the catalytic activity of enzymes immobilized on carbon nanotube electrodes was achieved by changing their local pH environment using electrochemical reactions.
Electrochemically stimulated molecular release from a modified electrode surface has been studied. The system was based on a buckypaper electrode modified with a molecular layer, which included a linker with a hydrolyzable phenolic ester bond connecting a fluorescent dye to the electrode surface, and with bilirubin oxidase catalyzing O2 reduction. The O2 reduction resulted in the local pH increase, which resulted in hydrolytic cleavage of the linker and release of the dye. The source of electrons for the reduction process can be electronic (potentiostat) or chemical (NADH). The potential applied on the modified electrode (0 V vs. Ag/AgCl) or generated in situ in the presence of NADH was very small, thus allowing the electrochemical process without complications of any side reaction. While the fluorescent dye released from the electrode represents a convenient model, various (bio)molecular species (e. g., drugs) can be released in the similar process. The designed signal‐controlled release system represents a general platform for various (bio)molecular delivering processes.
His‐tagged molecular species, a ferrocene derivative and Protein A, were immobilized on electrode surfaces (Au and graphite) through formation of a chelated complex in the presence of Cu2+ cations used as bridging units. The complex was cleaved and the attached molecules were released from the electrode surface by applying reductive potential to the electrodes resulting in Cu2+ reduction, thus decomposing the chelate complex. The molecule release process was followed by cyclic voltammetry in case of the ferrocene derivative. His‐tagged Protein A was additionally labeled with a fluorescent tag and its release was followed by fluorescence measurements in the solution and by impedance spectroscopy at the electrode. The studied release of the His‐tagged redox species and biomolecules was considered as a new generic approach to the signal‐controlled molecule release applicable in various biotechnological and biomedical applications.
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