Micromotors Powered by Enzyme Catalysis

TLDR

Active biocompatible systems are of great current interest for their possible applications in drug or antidote delivery at specific locations. Herein, we report the synthesis and study of self‑propelled microparticles powered by enzymatic reactions and their directed movement in a substrate concentration gradient. Polystyrene microparticles were functionalized with urease and catalase via biotin–streptavidin linkage, and their motion in the presence of substrates was examined by optical microscopy, dynamic light scattering, and a three‑inlet microfluidic channel to assess directed chemotaxis. The diffusion of the particles increased in a substrate‑concentration dependent manner.

Abstract

Active biocompatible systems are of great current interest for their possible applications in drug or antidote delivery at specific locations. Herein, we report the synthesis and study of self-propelled microparticles powered by enzymatic reactions and their directed movement in substrate concentration gradient. Polystyrene microparticles were functionalized with the enzymes urease and catalase using a biotin–streptavidin linkage procedure. The motion of the enzyme-coated particles was studied in the presence of the respective substrates, using optical microscopy and dynamic light scattering analysis. The diffusion of the particles was found to increase in a substrate concentration dependent manner. The directed chemotactic movement of these enzyme-powered motors up the substrate gradient was studied using three-inlet microfluidic channel architecture.