Lateral sorting in model membranes by cholesterol-mediated hydrophobic matching

Research output: Contribution to journalArticle


  • Hermann Josef Kaiser
  • Adam Orłowski
  • Tomasz Róg
  • Thomas K.M. Nyholm
  • Wengang Chai
  • Ten Feizi
  • Daniel Lingwood
  • Ilpo Vattulainen
  • Kai Simons

Research units

  • Max Planck Institute of Molecular Cell Biology and Genetics
  • Max Delbrück Center for Molecular Medicine in the Helmholtz Association
  • Tampere University of Technology
  • Åbo Akademi University
  • Imperial College London
  • Aalto University
  • University of Southern Denmark


Theoretical studies predict hydrophobic matching between transmembrane domains of proteins and bilayer lipids to be a physical mechanism by which membranes laterally self-organize. We now experimentally study the direct consequences of mismatching of transmembrane peptides of different length with bilayers of different thicknesses at the molecular level. In both model membranes and simulations we show that cholesterol critically constrains structural adaptations at the peptide-lipid interface under mismatch. These constraints translate into a sorting potential and lead to selective lateral segregation of peptides and lipids according to their hydrophobic length.


Original languageEnglish
Pages (from-to)16628-16633
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number40
Publication statusPublished - 4 Oct 2011
MoE publication typeA1 Journal article-refereed

    Research areas

  • Annular lipid, Mattress model, Membrane domain, Protein-lipid interaction, Self-assembly

ID: 17001272