Bulletin of the American Physical Society
APS March Meeting 2024
Monday–Friday, March 4–8, 2024; Minneapolis & Virtual
Session OD01: V: On-Demand Presentations - Available throughout March Meeting
6:00 AM,
Sunday, March 3, 2024
Abstract: OD01.00005 : Investigating chemotaxis in asymmetric liposomes*
Presenter:
Barbara Borges Fernandes
(Institute for Bioengineering of Catalonia (IBEC), The Barcelona Institute of Science and Technology (BIST))
Authors:
Barbara Borges Fernandes
(Institute for Bioengineering of Catalonia (IBEC), The Barcelona Institute of Science and Technology (BIST))
Subhadip Ghosh
(Institute for Bioengineering of Catalonia (IBEC), The Barcelona Institute of Science and Technology (BIST))
Ian Williams
(Department of Physics, University of Surrey)
Joe Forth
(Department of Chemistry, University of Liverpool)
Lorena Ruiz-Perez
(Institute for Bioengineering of Catalonia (IBEC), The Barcelona Institute of Science and Technology (BIST))
Giuseppe Battaglia
(Institute for Bioengineering of Catalonia (IBEC), The Barcelona Institute of Science and Technology (BIST))
This study investigates a novel active system composed of liposomes with encapsulated enzymes. Asymmetry is introduced by incorporating the pore protein alpha-hemolysin, facilitating the diffusion of substrate and products across the vesicle membrane. The resulting asymmetric distribution of species creates a slip velocity on the liposome's surface, resulting in self-propulsion.
The nature of the substrate proves to be a critical factor influencing the velocity and direction of the drift of liposomes in a microfluidic channel. Phenomena such as diffusioosmosis and diffusioosmophoresis emerge as inherent components of the motion we measured by tracking polystyrene beads with different surface chemistry in a gradient of urea and glucose. These phenomena are also present in the movement of porated liposomes. In addition to them, a chemotaxis component is observed for the liposomes that have pores. The drift direction and velocity result from all these events and depend on the enzyme/ substrate pair.
This research sheds light on some fundamental principles governing liposome chemotaxis with encapsulated enzymes. This system can offer insights into the chemotactic behavior of some natural vesicles and can also be applied in diverse fields, including drug delivery. The interplay between substrate properties, surface interactions, enzyme reactions, and asymmetry opens new horizons for further exploration of chemotaxis in biochemical systems.
*This project has received funding from the European Research Council (ERC) under the European Union's Horizon 2020 Research and Innovation Programme (grant agreement No 769798).
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