Molecular modeling of proteinlike inclusions in lipid bilayeMolecular modeling of proteinlike inclusions in lipid bilayers: lipid-mediated interactionss: Lipid-mediated interactions

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Abstract

We investigated the insertion of transmembrane structures in a lipid bilayer and their interactions using self-consistent field theory. The lipids are coarse-grained on a united-atom level and consist of a phosphatidylcholinelike headgroup and two hydrophobic tails. The inclusions, acting as simple models for proteins that span biological membranes, are rigid rods (radius R ) with a hydrophobic surface and hydrophilic end caps. The insertion free energy Omega of an individual rod is strongly regulated by the affinity between its hydrophobic surface and the lipid tails. This affinity also controls the best match of the hydrophobic length of the rod with that of the bilayer. The line tension tau(=Omega/2piR) is practically independent of R . The perturbations in the bilayer as a function of distance from the inclusion, have the shape of a damped oscillation. The wavelength and decay length are related to the elastic properties of the bilayer and do not depend on R . These results are used to analyze how the lipid matrix affects the interaction between transmembrane objects, for computational reasons considering the limit of R-->infinity . Contributions on different length scales can be distinguished: (i) a long-range elastic interaction, which is an exponentially decaying oscillation; (ii) an exponentially decaying repulsion on an intermediate length scale, resulting from the loss of conformational entropy of the lipid tails; and (iii) a short-range interaction due to the finite compressibility of the lipid tails, which manifests either as a depletion attraction if there is no affinity between the tails and the inclusions' surface or, otherwise, as an oscillatory structural force
Original languageEnglish
Article number021915
Number of pages12
JournalPhysical Review. E, Statistical nonlinear, and soft matter physics
Volume81
Issue number2
DOIs
Publication statusPublished - 2010

Keywords

  • membrane-induced interactions
  • transmembrane proteins
  • hydrophobic mismatch
  • boundary-conditions
  • enzymatic-activity
  • channel lifetime
  • chain-length
  • thickness
  • deformation
  • adsorption

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