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Distinct Network Morphologies from In Situ Polymerization of Microtubules in Giant Polymer-Lipid Hybrid Vesicles

Creating artificial cells with a dynamic cytoskeleton, akin to those in living cells, is a major goal in bottom-up synthetic biology. In this study, we demonstrate the in situ polymerization of microtubules encapsulated in giant polymer-lipid hybrid vesicles (GHVs) composed of 1,2-dioleoyl-sn-glycero-3-phosphocholine and an amphiphilic block copolymer. The block copolymer is comprised of poly(cholesteryl methacrylate-co-butyl methacrylate) as the hydrophobic block and either poly(6-O-methacryloyl-D-galactopyranose) or poly(carboxyethyl acrylate) as the hydrophilic extension. Depending on the concentrations of guanosine triphosphate (GTP) or its slowly hydrolyzable analog, guanosine-5′-[(α,β)-methyleno]triphosphate (GMPCPP), different microtubule morphologies are observed, including encapsulated microtubule networks, spike protrusions, as well as membrane-associated or aggregated microtubules. Overall, this work represents a step forward in mimicking the cellular cytoskeletons and uncovering the influence of membrane composition on microtubule morphologies.

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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

Marvian, A. T., Aliakbari, F., Mohammad-Beigi, H., Ahmadi, Z. A., Mehrpouyan, S., Lermyte, F., Nasouti, M., Collingwood, J. F., Otzen, D. E. & Morshedi, D. (2020). The status of the terminal regions of α-synuclein in different forms of aggregates during fibrillization. International Journal of Biological Macromolecules, 155, 543-550. https://doi.org/10.1016/j.ijbiomac.2020.03.238

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