Positive and negative chemotaxis of enzyme-coated liposome motors

Ambika Somasundar, Subhadip Ghosh, Farzad Mohajerani, Lynnicia N. Massenburg, Tinglu Yang, Paul S. Cremer, Darrell Velegol, Ayusman Sen

Research output: Contribution to journalArticlepeer-review

149 Scopus citations

Abstract

The ability of cells or cell components to move in response to chemical signals is critical for the survival of living systems. This motion arises from harnessing free energy from enzymatic catalysis. Artificial model protocells derived from phospholipids and other amphiphiles have been made and their enzymatic-driven motion has been observed. However, control of directionality based on chemical cues (chemotaxis) has been difficult to achieve. Here we show both positive or negative chemotaxis of liposomal protocells. The protocells move autonomously by interacting with concentration gradients of either substrates or products in enzyme catalysis, or Hofmeister salts. We hypothesize that the propulsion mechanism is based on the interplay between enzyme-catalysis-induced positive chemotaxis and solute–phospholipid-based negative chemotaxis. Controlling the extent and direction of chemotaxis holds considerable potential for designing cell mimics and delivery vehicles that can reconfigure their motion in response to environmental conditions.

Original languageEnglish
Pages (from-to)1129-1134
Number of pages6
JournalNature Nanotechnology
Volume14
Issue number12
DOIs
StatePublished - Dec 1 2019
Externally publishedYes

Funding

The work was supported by the Center for Chemical Innovation funded by the National Science Foundation (grant no. CHE-1740630). P.S.C. and D.V. acknowledge the National Science foundation for funding their work (grant nos. CHE-1709735 and CBET-1603716, respectively)

FundersFunder number
Center for Chemical Innovation
P.S.C.
National Science Foundation1709735, CBET-1603716, CHE-1709735, CHE-1740630, 1740630
National Science Foundation

    Fingerprint

    Dive into the research topics of 'Positive and negative chemotaxis of enzyme-coated liposome motors'. Together they form a unique fingerprint.

    Cite this