Lipid enrichment and selectivity of integral membrane proteins in two-component lipid bilayers

Research output: Contribution to journalJournal article

A model recently used to study lipid-protein interactions in one-component lipid bilayers (Sperotto and Mouritsen, 1991 a, b) has been extended in order to include two different lipid species characterized by different acyl-chain lengths. The model, which is a statistical mechanical lattice model, assumes that hydrophobic matching between lipid-bilayer hydrophobic thickness and hydrophobic length of the integral protein is an important aspect of the interactions. By means of Monte Carlo simulation techniques, the lateral distribution of the two lipid species near the hydrophobic protein-lipid interface in the fluid phase of the bilayer has been derived. The results indicate that there is a very structured and heterogeneous distribution of the two lipid species near the protein and that the protein-lipid interface is enriched in one of the lipid species. Out of equilibrium, the concentration profiles of the two lipid species away from the protein interface are found to develop a long-range oscillatory behavior. Such dynamic membrane heterogeneity may be of relevance for determining the physical factors involved in lipid specificity of protein function.

Original languageEnglish
JournalEuropean Biophysics Journal
Volume22
Issue number5
Pages (from-to)323-328
Number of pages6
ISSN0175-7571
DOIs
Publication statusPublished - 1 Nov 1993

    Research areas

  • Binary mixture, Lipid bilayer, Lipid selectivity, Lipidprotein interaction

ID: 236891135