title: Lateral sorting in model membranes by cholesterol-mediated hydrophobic matching.
abstract: 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.
authors.affiliation: Max Planck Institute for Molecular Cell Biology and Genetics, Pfotenhauerstr 108, 01307 Dresden, Germany.
authors.forename: Hermann-Josef
authors.initials: HJ
authors.lastname: Kaiser
authors.forename: Adam
authors.initials: A
authors.lastname: Orłowski
authors.forename: Tomasz
authors.initials: T
authors.lastname: Róg
authors.forename: Thomas K M
authors.initials: TK
authors.lastname: Nyholm
authors.forename: Wengang
authors.initials: W
authors.lastname: Chai
authors.forename: Ten
authors.initials: T
authors.lastname: Feizi
authors.forename: Daniel
authors.initials: D
authors.lastname: Lingwood
authors.forename: Ilpo
authors.initials: I
authors.lastname: Vattulainen
authors.forename: Kai
authors.initials: K
authors.lastname: Simons
mesh_terms: D002784:Cholesterol / Q000378:metabolism*; D057927:Hydrophobic and Hydrophilic Interactions; D008051:Lipid Bilayers / Q000378:metabolism*; D008565:Membrane Proteins / Q000378:metabolism*; D008954:Models, Biological; D056004:Molecular Dynamics Simulation
chemical_list: D008051:Lipid Bilayers; D008565:Membrane Proteins; D002784:Cholesterol