Artificial muscle reversibly controlled by enzyme reactions

Chemically induced actuation of a polypyrrole (Ppy) artificial muscle was controlled by biocatalytic reactions, resulting in changes in the redox state of the polymer film mediated by soluble redox species. The biocatalytic process triggered by diaphorase in the presence of NADH resulting in the reduction of the Ppy film was reflected by the potential shift in the negative direction generated in the film. Conversely, the biocatalytic process driven by laccase in the presence of O₂ resulted in the oxidation of the Ppy film, thus yielding the positive potential shift. Both reactions produced opposite bending of the Ppy flexible strip, allowing reversible actuation controlled by the biocatalytic processes. The biocatalytic reactions governing the chemical actuator can be extended to multistep cascades processing various patterns of biochemical signals and mimicking logic networks. The present chemical actuator exemplifies the first mechanochemical device controlled by biochemical means with the possibility to scale up the complexity of the biochemical signal-processing system.