Lateral sorting in model membranes by cholesterol-mediated hydrophobic matching

Tutkimustuotos: Lehtiartikkelivertaisarvioitu


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


  • 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.


JulkaisuProceedings of the National Academy of Sciences of the United States of America
TilaJulkaistu - 4 lokakuuta 2011
OKM-julkaisutyyppiA1 Julkaistu artikkeli, soviteltu

ID: 17001272