Search bioRxiv⌕ Search

bioRxiv · 10.64898/2026.10.26.761816

Structural Determinants of the Energetic Barrier of Phospholipid Flip-Flop

Abstract

Spontaneous phospholipid flip-flop sets the background against which flippases, floppases, and scramblases create and dissipate membrane asymmetry. How the associated free-energy barrier depends on lipid chemistry and on the surrounding membrane remains unclear, because experiments are few and contradictory and previous simulations covered only a small part of the lipidome. Here, we calculate Martini 3 flip-flop free-energy barriers for over 700 membrane--lipid combinations, the largest such dataset to our knowledge. A systematic single component bilayer panel of five headgroups, three linkages, and 35 tail families is complemented by mixed bilayers, from binary mixtures to organelle-inspired compositions, that place the same lipid in different membranes and thus separate the effects of lipid chemistry and the membrane environment. In single component bilayers, the barrier rises with tighter tail packing and depends strongly on headgroup and tail unsaturation but only weakly on linkage. Moving a lipid into a mixed bilayer shifts its barrier as much as most headgroup substitutions do, and the shift follows the change in local tail order. Within a shared membrane, headgroup differences are mostly smaller than between single component bilayers, so part of a headgroup effect arises from the membrane that the lipid forms. A Bayesian model combining chemical descriptors with local membrane structure predicts barriers for withheld lipid families and membranes with cross-validated errors of 2.8 and 3.8 kJ/mol. The calculated trends agree qualitatively with native-lipid vesicle experiments, although Martini 3 underestimates the barrier differences between lipids, gives lower barriers than atomistic models, and overstates the effect of cholesterol.

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

Vuorte, M. I., Pandey, U., Javanainen, M.. 2026-10-26. Structural Determinants of the Energetic Barrier of Phospholipid Flip-Flop. https://doi.org/10.64898/2026.10.26.761816

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related preprints

Cancers relax selection on charge at the mitochondrial complex I quinone cavity

Mitochondrial complex I translocates protons through hydrated channels whose connectivity and electrostatics are both defined by structure, but whether they are distinctly constrained is unknown. From a 2.39 cryo-EM structure modelling 2,945 ordered waters, we built the proton wire of the seven mtDNA-encoded ND subunits and scored all 40,166 missense substitutions on two near-orthogonal axes (r = 0.17): electrostatic shift at proton-loading sites, and topological disruption of the wire. Across 858 germline variant sites, loading sites (0.51) and cut vertices (0.67) are both depleted. In tumours only loading sites are enriched (1.42 TCGA, 1.67 PCAWG, 1.29 MSK-IMPACT), a 3.06-fold difference tested as a wire class tissue-type interaction (P = 3.6 10-). It survives adjustment for conservation, burial and coverage, and is concentrated in ND1 within 15 of the quinone cavity, not spread along the proton path. Selection separates charge from connectivity, without establishing a fitness benefit.

biophysics↗

Rugnux: from diffraction images to structure at synchrotrons and XFELs in one program

Rising data rates in macromolecular crystallography outpace multi-program pipelines on computing clusters. Rugnux, a single GPU-accelerated program, turns rotation or serial still diffraction images into merged data and an initial structure. At synchrotrons, results arrive seconds after the last image; on one workstation, 207 public datasets from 36 sources took a median of 15 s each, with deposition-quality. Serial XFEL data were processed faster than the collection rate, enabling real-time structure determination.

biophysics↗

Phase Separation of Intracellular Proteins Influences Synaptic Bistability

Synaptic bistability at the post synaptic density has been proposed to be the result of the nucleation and evaporation of receptor clusters. The exact biophysical mechanism underlying these inter-receptor attractions that can trigger nucleation remains to be elucidated. Emerging evidence demonstrates that numerous postsynaptic density submembrane proteins, that interact with various membrane receptors, can undergo phase separation, necessitating a revised conceptual model. By employing Langevin dynamics simulations of coarse-grained scaffold proteins and interacting membrane receptors, we study how phase transitions of scaffold proteins alter receptor clustering at the membrane. In our model, scaffold macromolecules can undergo phase separation and interact with receptor molecules at the model membranes. We observed that the presence of scaffold polymers across the membrane creates an attractive interaction between otherwise purely repulsive receptors. By systematically varying the number of receptors at the membrane, we dissected the coupling between receptor clustering and the phase behavior of scaffold macromolecules. We show that the propensity for receptor clustering is enhanced by the condensation of scaffold proteins. We then used two different scaffolds and systematically varied the interaction between them, to change the spatial organization of two condensed phases w.r.t. one another. Interestingly, we observed that receptor clustering can be reduced by co-phase separation of scaffold macromolecules, indicating the role of competing interactions in receptor clustering. Our work advances understanding of receptor-mediated signaling and phase separation, providing insights into cellular compartmentalization and biochemical regulation at the synapse.

biophysics↗