Electrochemically produced local pH changes stimulating (bio)molecule release from pH-switchable electrode-immobilized avidin-biotin systems.

Immobilized avidin-biotin complexes were used to release biotinylated (bio)molecules upon producing local pH changes near an electrode surface by electrochemical reactions. The nitro-avidin complex with biotin was dissociated by increasing local pH with electrochemical O2 reduction. The avidin complex with iminobiotin was split by decreasing local pH with electrochemical oxidation of ascorbate. Both studied systems were releasing molecule cargo species in response to small electrical potentials (-0.4 V or 0.2 V for the O2 reduction or ascorbate oxidation, respectively) applied on the modified electrodes.

Boolean Logic Networks Mimicked with Chimeric Enzymes Activated/Inhibited by Several Input Signals.

The front cover artwork is provided by groups of Prof. Evgeny Katz and Prof. Artem Melman (Clarkson University, NY, USA) as well as Prof. Kirill Alexandrov (Queensland University of Technology, Brisbane, Australia). The image shows activation/inhibition of a chimeric enzyme with biomolecular signals and a corresponding logic network - the artistic vision. Read the full text of the Communication at 10.1002/cphc.201901050.

Boolean Logic Networks Mimicked with Chimeric Enzymes Activated/Inhibited by Several Input Signals.

Reactions catalyzed by artificial allosteric enzymes, chimeric proteins with fused biorecognition and catalytic units, were used to mimic multi-input Boolean logic systems. The catalytic parts of the systems were represented by pyrroloquinoline quinone-dependent glucose dehydrogenase (PQQ-GDH). Two biorecognition units, calmodulin or artificial peptide-clamp, were integrated into PQQ-GDH and locked it in the OFF or ON state respectively. The ligand-peptide binding cooperatively with Ca2+ cations to a calmodulin bioreceptor resulted in the enzyme activation, while another ligand-peptide bound to a clamp-receptor inhibited the enzyme. The enzyme activation and inhibition originated from peptide-induced allosteric transitions in the receptor units that propagated to the catalytic domain. While most of enzymes used to mimic Boolean logic gates operate with two inputs (substrate and co-substrate), the used chimeric enzymes were controlled by four inputs (glucose - substrate, dichlorophenolindophenol - electron acceptor/co-substrate, Ca2+ cations and a peptide - activating/inhibiting signals). The biocatalytic reactions controlled by four input signals were considered as logic networks composed of several concatenated logic gates. The developed approach allows potentially programming complex logic networks operating with various biomolecular inputs representing potential utility for different biomedical applications.

Electrochemical control of the catalytic activity of immobilized enzymes.

Regulation of the catalytic activity of enzymes immobilized on carbon nanotube electrodes was achieved by changing their local pH environment using electrochemical reactions. Reduction of oxygen increased the interfacial pH while oxidation of ascorbate decreased it, thus allowing changing rates of enzymatic reactions of electrode-immobilized amyloglucosidase and trypsin enzymes over a wide activity range.

Electrochemically stimulated molecule release associated with interfacial pH changes.

A new linker with a hydrolyzable aryl ester bond was used for electrode modification. Basic pH locally produced at the electrode surface upon electrochemical reduction of O2 resulted in the hydrolytic cleavage of the aryl ester bond and release of the immobilized fluorescent dye used as a model compound.