Micromotors powered by enzyme catalysis

Dey, K. K.; Zhao, X.; Tansi, B. M.; Méndez-Ortiz, J. W.; Córdova-Figueroa, U. M.; Golestanian, R.; Sen, A.

doi:10.1021/acs.nanolett.5b03935

Item

ITEM ACTIONSEXPORT

Add to Basket

Local TagsRelease HistoryDetailsSummary

Released

Journal Article

Micromotors powered by enzyme catalysis

MPS-Authors

/persons/resource/persons219873

Golestanian, R.
Department of Living Matter Physics, Max Planck Institute for Dynamics and Self-Organization, Max Planck Society;

External Resource

No external resources are shared

Fulltext (restricted access)

There are currently no full texts shared for your IP range.

Fulltext (public)

There are no public fulltexts stored in PuRe

Supplementary Material (public)

There is no public supplementary material available

Citation

Dey, K. K., Zhao, X., Tansi, B. M., Méndez-Ortiz, J. W., Córdova-Figueroa, U. M., Golestanian, R., et al. (2015). Micromotors powered by enzyme catalysis. Nano Letters, 15(12), 8311-8315. doi:10.1021/acs.nanolett.5b03935.

Cite as: https://hdl.handle.net/21.11116/0000-0001-A796-9

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. © 2015 American Chemical Society.