ArticleNanoscale advances2021
Development, structure and mechanics of a synthetic
Article in Nanoscale advances, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Single-cell analysis of lipopolysaccharide-mediated heterogeneity in Escherichia coli adhesion and mechanics.Archives of microbiology · 2025Article
- Advancements in Escherichia coli secretion systems for enhanced recombinant protein production.World journal of microbiology & biotechnology · 2025Review
- The Effect of Lipopolysaccharides fromBiomimetics (Basel, Switzerland) · 2025Article
- Nanostructural and nanomechanical alterations of photosensitized lipid membranes due to light induced formation of reactive oxygen species.Scientific reports · 2025Article
- Article
- Model architectures for bacterial membranes.Biophysical reviews · 2022Review
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Authors and funding
6 authors.
Funding
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Abstract
The outer membrane (OM) of Gram-negative bacteria is a complex asymmetric bilayer containing lipids, lipopolysaccharides (LPS) and proteins. While it is a mechanical and chemical barrier, it is also the primary surface of bacterial recognition processes that involve infection by and of the bacterium. Uncovering the mechanisms of these biological functions has been hampered by the lack of suitable model systems. Here we report the step-by-step assembly of a synthetic OM model from its fundamental components. To enable the efficient formation of a supported lipid bilayer at room temperature, dimyristoyl-phosphocholine (DMPC) was used as the lipid component to which we progressively added LPS and OM proteins. The assembled system enabled us to explore the contribution of the molecular components to the topographical structure and stability of the OM. We found that LPS prefers solid-state membrane regions and forms stable vesicles in the presence of divalent cations. LPS can gradually separate from DMPC membranes to form independent vesicles, pointing at the dynamic nature of the lipid-LPS system. The addition of OM proteins from
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Registered trials
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