Demixing of homogeneous binary lipid membranes induced by protein inclusions

Nowakowski, Piotr; Stumpf, Bernd Henning; Smith, Ana‐Sunčana; Maciołek, Anna

doi:10.1103/physreve.107.054120

Cited by 2 publications

(1 citation statement)

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“…There is extensive literature on how particles—nearby, attached, or inserted into a membrane—affect membrane shape. Examples include the effects of different types of lipids [21–30] polymers [31–35] nanoparticles [36–40] phospholipid-surfactant mixtures [41], protein pumps [20, 42], adsorbed BAR proteins [43–48] inter-calated curvature-inducing proteins [49–51] and crowds of sterically-repelling proteins [52–56] (see also reviews in [57–59] Generally speaking, the total free energy of such systems contains, besides the Helfrich free energy, the free energy of the particles and a term accounting for the interaction of the membrane with the particles. Expressions for the free energy of the particles often contain terms penalising phase boundaries [22, 41, 43, 49, 60] and terms accounting for interactions between the particles and for entropy, either through a Flory-Huggins theory for a mixture of occupied and unoccupied sites [21, 27, 33, 41, 43], or a Ginzburg-Landau expansion thereof [22, 49, 61].…”

Section: Introductionmentioning

confidence: 99%

Stability of a biomembrane tube covered with proteins

Janssen

Liese

Carlson

2022

Preprint

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Membrane tubes are essential structural features in cells that help facilitate biomaterial transport and inter- and intracellular signalling. The shape of these tubes can be regulated by the proteins that surround and adhere to them. We study here the stability of a biomembrane tube coated with proteins by combining linear stability analysis and numerical solutions of a Helfrich-like membrane model. Our analysis demonstrates that both long and short wavelength perturbations can destabilise the tubes. Numerical simulations confirm the derived linear stability criteria and also yield the nonlinearly-perturbed vesicle shapes. Our analysis highlights the interplay between the membrane shape and the protein density, where the shape instability concurs with a redistribution of proteins into a banded pattern.

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Section: Introductionmentioning

confidence: 99%

Stability of a biomembrane tube covered with proteins

Janssen

Liese

Carlson

2022

Preprint

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Hydrophobic mismatch drives self-organization of designer proteins into synthetic membranes

Peruzzi,

Steinkühler,

et al. 2024

Nat Commun

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The organization of membrane proteins between and within membrane-bound compartments is critical to cellular function. Yet we lack approaches to regulate this organization in a range of membrane-based materials, such as engineered cells, exosomes, and liposomes. Uncovering and leveraging biophysical drivers of membrane protein organization to design membrane systems could greatly enhance the functionality of these materials. Towards this goal, we use de novo protein design, molecular dynamic simulations, and cell-free systems to explore how membrane-protein hydrophobic mismatch could be used to tune protein cotranslational integration and organization in synthetic lipid membranes. We find that membranes must deform to accommodate membrane-protein hydrophobic mismatch, which reduces the expression and co-translational insertion of membrane proteins into synthetic membranes. We use this principle to sort proteins both between and within membranes, thereby achieving one-pot assembly of vesicles with distinct functions and controlled split-protein assembly, respectively. Our results shed light on protein organization in biological membranes and provide a framework to design self-organizing membrane-based materials with applications such as artificial cells, biosensors, and therapeutic nanoparticles.

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Demixing of homogeneous binary lipid membranes induced by protein inclusions

Cited by 2 publications

References 65 publications

Stability of a biomembrane tube covered with proteins

Stability of a biomembrane tube covered with proteins

Hydrophobic mismatch drives self-organization of designer proteins into synthetic membranes

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