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BP: Fachverband Biologische Physik

BP 8: Poster Session Ia

BP 8.27: Poster

Montag, 18. März 2024, 18:00–20:30, Poster C

Fungal hydrophobins as building blocks for rigid, water-impermeable pure protein bilayers and vesicles — Friederike Nolle, Kirstin Kochems, Karin Jacobs, and •Hendrik Hähl — Experimental Physics & Center for Biophysics, Saarland University, Saarbrücken, Germany

Hydrophobins are a class of small, strongly amphiphilic and extremely stable proteins formed mainly by filamentous fungi. Similar to surfactant molecules like phospholipids they self-assemble in monolayer films at water interfaces. Contacting two films, stable membranes resembling lipid bilayers are obtained, and subsequently also vesicles can be formed. These hydrophobin bilayers exhibit a similar thickness to lipid bilayers allowing for an incorporation of simple ion channels [1].

Due to their natural biocompatibility, higher stability in comparison to lipid bilayers and versatility gained through bioengineering, the application potential for hydrophobin bilayers and vesicles is vast. Many properties of this new type of membrane are, however, still to be characterized. We report here on mechanical testing via atomic force microscopy on pore-spanning films and determination of the water permeability in a droplet interface bilayer setup. We find that the layers exhibit a finite elasticity and high stability, withstand by far larger osmotic pressures than lipid bilayers, and are nearly impermeable to water [2]. Yet, by disturbing the molecular packing in the bilayer, the permeability can be tuned.

[1] H. Hähl et al., Adv Mater 29, 1602888 (2017).

[2] F. Nolle et al., Langmuir 39, 13790 (2023).

Keywords: Hydrophobin; bilayer; membrane; water permeability