The European Physical Journal E

, Volume 14, Issue 3, pp 299–308

Tilt modulus of a lipid monolayer


    • Junior Research Group “Lipid Membranes”Friedrich-Schiller-Universität Jena
  • Y. Kozlovsky
    • Department of Physiology and Pharmacology, Sackler Faculty of MedicineTel-Aviv University
  • A. Ben-Shaul
    • Department of Physical Chemistry and the Fritz Haber Research CenterThe Hebrew University
  • M. M. Kozlov
    • Department of Physiology and Pharmacology, Sackler Faculty of MedicineTel-Aviv University

DOI: 10.1140/epje/i2004-10019-y

Cite this article as:
May, S., Kozlovsky, Y., Ben-Shaul, A. et al. Eur. Phys. J. E (2004) 14: 299. doi:10.1140/epje/i2004-10019-y


In addition to the familiar bending and stretching deformations, lipid monolayers and bilayers in their disordered state are often subjected to tilt deformations, occurring for instance in structural rearrangements accompanying membrane fusion, or upon insertion of “oblique” hydrophobic proteins into lipid bilayers. We study the elastic response of a flat lipid monolayer to a tilt deformation, using the spatial and conformational average of the chain end-to-end vector from the membrane normal to define a macroscopic membrane tilt. The physical origin and magnitude of the corresponding tilt modulus \(\kappa_t\) is analyzed using two complementary theoretical approaches. The first is a phenomenological model showing that the tilt and bending deformations are decoupled and the effects of inter-chain correlations on the tilt modulus is small. The second is based on a molecular-level mean-field theory of chain packing, enabling numerical evaluation of the tilt modulus for realistic, multi-conformation, chain models. Both approaches reveal that the tilt modulus involves two major contributions. The first is elastic in origin, arising from the stretching of the hydrocarbon chains upon a tilt deformation and reflecting the loss of chain conformational freedom associated with chain stretching. The second, purely entropic, contribution results from the constraints imposed by a tilt deformation on the fluctuations of chain director orientations. Using the chain-packing theory we compute the two contributions numerically as a function of the cross-sectional area per chain. The elastic and entropic terms are shown to dominate the value of \(\kappa_t\) for small and large areas per chain, respectively. For typical cross-sectional areas of lipid chains in biological membranes they areof comparable magnitude, yielding \(\kappa_t \approx 0.2k_{\rm B}T/\AA^2\).

Copyright information

© Springer-Verlag Berlin/Heidelberg 2004