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Single Protein-Mediated Vesicle Division

Steering group member of AUNAB, Prof. Brigitte Städler, has published a collaborative study in Advanced Materials on the successful reconstitution of the Drs2p–Cdc50p lipid flippase in polymer–lipid hybrid vesicles.

The successful reconstitution of Drs2p–Cdc50p flippase in small and giant polymer lipid hybrid vesicles is illustrated. The hybrid vesicles show adenosine 5′-triphosphate consumption and flipping of 2-dioleoyl-sn-glycero-3-phospho-l-serine lipids from the inner to the outer leaflet. This induced transmembrane asymmetry results in constriction and division of the giant hybrid vesicles.

A collaborative study between the Lyons and Stadler labs, published in Advanced Materials, reports the successful reconstitution of the Drs2p–Cdc50p lipid flippase in polymer–lipid hybrid vesicles, enabling active translocation of negatively charged lipids to establish transmembrane asymmetry. Crucially, the chemical nature of the hydrophobic block in the amphiphilic block copolymers determines the curvature changes that drive vesicle constriction and division. This work marks an important step toward constructing synthetic systems capable of protein-mediated division, advancing the goal of bottom-up self-replicating assemblies.

Read the article published in Advanced Marterials here.

Contact information:
Professor Brigitte Maria Städler
Aarhus University
Interdisciplinary Nanoscience Center (iNANO)
Email: bstadler@inano.au.dk

Tenure track Assistant Professor Joseph Lyons
Aarhus University
Interdisciplinary Nanoscience Center (iNANO)
Email: lyons@inano.au.dk

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Golan, N., Parizat, A., Tabachnikov, O., Barnea, E., Olsen, W. P., Otzen, D. E. & Landau, M. (2025). Resilience and Charge-Dependent Fibrillation of functional amyloid: Interactions of Pseudomonas Biofilm-Associated FapB and FapC Amyloids. The Journal of Biological Chemistry, 301(2), Article 108096. https://doi.org/10.1016/j.jbc.2024.108096
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