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AUNAB - Aarhus University Network on Artificial Biology

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Recent research news on Artificial Biology

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.

4 September 2025 by Emilia Djomina Hansen

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

Recent publications by network

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Hansen, B. K., Larsen, C. K., Nielsen, J. T., Svenningsen, E. B., Van, L. B., Jacobsen, K. M., Bjerring, M., Flygaard, R. K., Jenner, L. B., Nejsum, L. N., Brodersen, D. E., Mulder, F. A. A., Tørring, T. & Poulsen, T. B. (2020). Structure and Function of the Bacterial Protein Toxin Phenomycin. Structure, 28(5), 528-539.e9. https://doi.org/10.1016/j.str.2020.03.003

Jensen, R. K., Jabs, F., Miehe, M., Mølgaard, B., Pfützner, W., Möbs, C., Spillner, E. & Andersen, G. R. (2020). Structure of intact IgE and the mechanism of ligelizumab revealed by electron microscopy. Allergy: European Journal of Allergy and Clinical Immunology, 75(8), 1952-1961. https://doi.org/10.1111/all.14222

Pedersen, J. N., Frislev, H. K. S., Pedersen, J. S. & Otzen, D. (2020). Structures and mechanisms of formation of liprotides. Biochimica et Biophysica Acta - Proteins and Proteomics, 1868(11), Article 140505. https://doi.org/10.1016/j.bbapap.2020.140505

Zhang, F., Kang, H., Lin, Y., Guan, L., Aslan, H., Zhang, M., Niu, L. & Dong, M. (2020). Studying the Pyroelectric Effects of LiNbO₃ Modified Composites. Nanoscale Research Letters, 15(1), Article 106. https://doi.org/10.1186/s11671-020-03341-w

Basse-O'Connor, A. (2020). Sufficient conditions for càdlàg sample paths of stable superpositions of Ornstein–Uhlenbeck processes. In Proceeding of the 62nd ISI World Statistics Congress 2019 (pp. 74–79). Department of Statistics Malaysia. http://isi2019.org/proceeding/2.STS/STS%20VOL%203/index.html#p=85

Campisi, D., Simonsen, F. D. S., Thrower, J. D., Jaganathan, R., Hornekær, L., Martinazzo, R. & Tielens, A. G. G. M. (2020). Superhydrogenation of pentacene: The reactivity of zigzag-edges. Physical Chemistry Chemical Physics, 22(3), 1557-1565. https://doi.org/10.1039/c9cp05440e

Rauber, M., Roßbach, A., Jung, A., Müller, S., Möbs, C., Pfützner, W., Miehe, M., Spillner, E. & Jakob, T. (2020). The honey bee venom allergen Api m 10 displays one major IgE epitope, Api m 10160-174. Allergy: European Journal of Allergy and Clinical Immunology, 75(7), 1756-1759. https://doi.org/10.1111/all.14187

Jakob, T., Rauber, M. M., Perez-Riverol, A., Spillner, E. & Blank, S. (2020). The Honeybee Venom Major Allergen Api m 10 (Icarapin) and Its Role in Diagnostics and Treatment of Hymenoptera Venom Allergy. Current Allergy and Asthma Reports, 20(9), Article 48. https://doi.org/10.1007/s11882-020-00943-3

van Gils, J. H. M., van Dijk, E., Peduzzo, A., Hofmann, A., Vettore, N., Schützmann, M. P., Groth, G., Mouhib, H., Otzen, D. E., Buell, A. K. & Abeln, S. (2020). The hydrophobic effect characterises the thermodynamic signature of amyloid fibril growth. PLoS Computational Biology, 16(5), Article e1007767. https://doi.org/10.1371/journal.pcbi.1007767

van Diggelen, F., Frank, S. A., Somavarapu, A. K., Scavenius, C., Apetri, M. M., Nielsen, J., Tepper, A. W. J. W., Enghild, J. J. & Otzen, D. E. (2020). The interactome of stabilized α-synuclein oligomers and neuronal proteins. FEBS journal, 287(10), 2037-2054. https://doi.org/10.1111/febs.15124

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Kalinka Hansen