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  Molecular dynamics simulations show that short peptides can drive synthetic cell division by binding to the inner membrane leaflet

Steinkühler, J., Lipowsky, R., & Miettinen, M. S. (2024). Molecular dynamics simulations show that short peptides can drive synthetic cell division by binding to the inner membrane leaflet. The Journal of Physical Chemistry B, 128(36), 8782-8787. doi:10.1021/acs.jpcb.4c04358.

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 Urheber:
Steinkühler, Jan, Autor
Lipowsky, Reinhard1, Autor                 
Miettinen, Markus S., Autor
Affiliations:
1Reinhard Lipowsky, Theorie & Bio-Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_1863327              

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 Zusammenfassung: An important functionality of lifelike “synthetic cells” is to mimic cell division. Currently, specialized proteins that induce membrane fission in living cells are the primary candidates for dividing synthetic cells. However, interactions between lipid membranes and proteins that are not found in living cells may also be suitable. Here, we discuss the potential of short membrane-anchored peptides to induce cell division. Specifically, we used the coarse-grained MARTINI model to investigate the interaction between short membrane-anchored peptides and a lipid bilayer patch. The simulation revealed that the anchored peptide induces significant spontaneous curvature and suggests that the lipid–peptide complex can be considered as a conically shaped “bulky headgroup” lipid. By systematically increasing the electrostatic charge of the peptide, we find that membrane-anchored peptides may generate sufficiently large constriction forces even at dilute coverages. Finally, we show that when the peptide has an opposite charge to the membrane, the peptide may induce division by binding the inner membrane leaflet of a synthetic cell, that is, cell division from within.

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Sprache(n): eng - English
 Datum: 2024-09-022024
 Publikationsstatus: Erschienen
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 Identifikatoren: DOI: 10.1021/acs.jpcb.4c04358
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Titel: The Journal of Physical Chemistry B
  Kurztitel : J. Phys. Chem. B
Genre der Quelle: Zeitschrift
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Ort, Verlag, Ausgabe: Washington, D.C. : American Chemical Society
Seiten: - Band / Heft: 128 (36) Artikelnummer: - Start- / Endseite: 8782 - 8787 Identifikator: ISSN: 1520-6106