Effect of intermonolayer coupling on the phase behavior of lipid bilayers

A statistical-mechanical lattice model is proposed to describe the acyl-chain main phase transition in a hydrated lipid bilayer. The model is built on a two-dimensional multistate lattice model to describe the intramonolayer interactions within the two separate lipid monolayers of the bilayer. The coupling between the two monolayers is modeled both indirectly by hydrophobic acyl-chain mismatch interactions that ensure compatibility between the two monolayers, and by a direct intermonolayer attractive dispersion force. The nature of the phase transition is studied by computer-simulation methods involving standard Monte Carlo simulation, as well as the extrapolation method of Ferrenberg and Swendsen [Phys. Rev. Lett. 61, 2635 (1988)] and the Lee-Kosterlitz technique [Phys. Rev. Lett. 65, 137 (1990); Phys. Rev. B 43, 3265 (1991)]. It is found that the absence of a phase transition in a set of uncoupled monolayers is restored by a weak intermonolayer interaction. The bilayer properties in the transition region are described with particular emphasis on the lateral density fluctuations and the resulting dynamic bilayer heterogeneity. The theoretical results are discussed in relation to experimental data

A Monte Carlo simulation study of protein-induced heat capacity changes and lipid-induced protein clustering.

Monte Carlo simulations were used to describe the interaction of peripheral and integral proteins with lipids in terms of heat capacity profiles and protein distribution. The simulations were based on a two-state model for the lipid, representing the lipid state as being either gel or fluid. The interaction between neighboring lipids has been taken into account through an unlike nearest neighbor free energy term delta omega, which is a measure of the cooperativity of the lipid transition. Lipid/protein interaction was considered using the experimental observation that the transition midpoints of lipid membranes are shifted upon protein binding, a thermodynamic consequence of different binding constants of protein with fluid or gel lipids. The difference of the binding free energies was used as an additional parameter to describe lipid-protein interaction. The heat capacity profiles of lipid/protein complexes could be well described for both peripheral and integral proteins. Binding of proteins results in a shift and an asymmetric broadening of the melting profile. The model results in a coexistence of gel and fluid lipid domains in the proximity of the thermotropic transition. As a consequence, bound peripheral proteins aggregate in the temperature range of the lipid transition. Integral proteins induce calorimetric melting curves that are qualitatively different from that of peripheral proteins and aggregate in either gel or liquid crystalline lipid phase. The results presented here are in good agreement with calorimetric experiments on lipid-protein complexes and have implementations for the functional control of proteins

Simulation of the gel-fluid transition in a membrane composed of lipids with two connected acyl chains: application of a dimer-move step.

Phospholipids have been treated as dimers on a hexagonal lattice, and a move has been introduced that allows the dimers to move and change their orientation on the lattice. Simulations have been performed in which phospholipid chains have been treated as being either independent or infinitely coupled thermodynamically with regard to their conformational state. Both types of simulation have reproduced well experimental heat-capacity curves of dipalmitoyl phosphatidylcholine small unilamellar vesicles. Apart from a different gel-fluid interaction parameter and a different number of unlike nearest-neighbor contacts, most of the averages and thermodynamic quantities were essentially the same in the two types of simulation. These results indicate that the transition is not first order and validate those of previous Monte Carlo simulations that have neglected the dimeric nature of phospholipids in the sense that they show that for the thermotropic transition the approximation of phospholipids as monomers is valid