Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 2010 Dec 15;99(12):L91-3.
doi: 10.1016/j.bpj.2010.08.072.

Partitioning of lipids at domain boundaries in model membranes

Lars V Schäfer  1 , Siewert J Marrink
Affiliations

Partitioning of lipids at domain boundaries in model membranes

Lars V Schäfer et al. Biophys J. .

Abstract

Line-active molecules ("linactants") that bind to the boundary interface between different fluid lipid domains in membranes have a strong potential as regulators of the lateral heterogeneity that is important for many biological processes. Here, we use molecular dynamics simulations in combination with a coarse-grain model that retains near-atomic resolution to identify lipid species that can act as linactants in a model membrane that is segregated into two lipid domains of different fluidity. Our simulations predict that certain hybrid saturated/unsaturated chain lipids can bind to the interface and lower the line tension, whereas cone-shaped lysolipids have a less pronounced effect.

PubMed Disclaimer

Figures

Figure 1
Figure 1
(a) The simulated lipid bilayer is segregated into an ordered (Lo) and a disordered (Ld) domain. The system comprises ∼2000 lipids, solvated by water (not shown). (b) Snapshot from simulation showing a part of the domain boundary interface. (c) MARTINI CG representations of DPPC (cyan), DLiPC (red), cholesterol (gray), and POPC (orange).
Figure 2
Figure 2
Lateral composition profiles along the dimension perpendicular to the domain boundaries (black dotted lines). The profiles obtained for the two bilayer leaflets are shown as dashed lines; solid lines represent the average. (a) POPC lipids (orange) accumulate close to the domain boundary. (b) PLiPC segregates into the Ld domain, whereas LysoPC (c) has a weak preference for the domain boundary interface.
See this image and copyright information in PMC

Similar articles

See all similar articles

Cited by

See all "Cited by" articles

References

    1. Simons K., Ikonen E. Functional rafts in cell membranes. Nature. 1997;387:569–572. - PubMed
    1. Hancock J.F. Lipid rafts: contentious only from simplistic standpoints. Nat. Rev. Mol. Cell Biol. 2006;7:456–462. - PMC - PubMed
    1. Kahya N., Scherfeld D., Schwille P. Probing lipid mobility of raft-exhibiting model membranes by fluorescence correlation spectroscopy. J. Biol. Chem. 2003;278:28109–28115. - PubMed
    1. Veatch S.L., Polozov I.V., Keller S.L. Liquid domains in vesicles investigated by NMR and fluorescence microscopy. Biophys. J. 2004;86:2910–2922. - PMC - PubMed
    1. Baumgart T., Hess S.T., Webb W.W. Imaging coexisting fluid domains in biomembrane models coupling curvature and line tension. Nature. 2003;425:821–824. - PubMed

Publication types

LinkOut - more resources