Lateral sorting in model membranes by cholesterol-mediated hydrophobic matching.

Hermann-Josef Kaiser, Adam Orłowski, Tomasz Róg, Thomas Nyholm, Wengang Chai, Ten Feizi, Daniel Lingwood, Ilpo Vattulainen, Kai Simons

Forskningsoutput: TidskriftsbidragArtikelVetenskapligPeer review

118 Citeringar (Scopus)


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.
Sidor (från-till)16628–16633
TidskriftProceedings of the National Academy of Sciences
StatusPublicerad - 2011
MoE-publikationstypA1 Tidskriftsartikel-refererad

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