Lateral sorting in model membranes by cholesterol-mediated hydrophobic matching

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Lateral sorting in model membranes by cholesterol-mediated hydrophobic matching. / Kaiser, Hermann Josef; Orłowski, Adam; Róg, Tomasz; Nyholm, Thomas K.M.; Chai, Wengang; Feizi, Ten; Lingwood, Daniel; Vattulainen, Ilpo; Simons, Kai.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 108, No. 40, 04.10.2011, p. 16628-16633.

Research output: Contribution to journalArticleScientificpeer-review

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Kaiser, HJ, Orłowski, A, Róg, T, Nyholm, TKM, Chai, W, Feizi, T, Lingwood, D, Vattulainen, I & Simons, K 2011, 'Lateral sorting in model membranes by cholesterol-mediated hydrophobic matching' Proceedings of the National Academy of Sciences of the United States of America, vol. 108, no. 40, pp. 16628-16633. https://doi.org/10.1073/pnas.1103742108

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Kaiser, Hermann Josef ; Orłowski, Adam ; Róg, Tomasz ; Nyholm, Thomas K.M. ; Chai, Wengang ; Feizi, Ten ; Lingwood, Daniel ; Vattulainen, Ilpo ; Simons, Kai. / Lateral sorting in model membranes by cholesterol-mediated hydrophobic matching. In: Proceedings of the National Academy of Sciences of the United States of America. 2011 ; Vol. 108, No. 40. pp. 16628-16633.

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@article{f9e6e8bd923749c5a0ad5efd0fd6bd89,
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.",
keywords = "Annular lipid, Mattress model, Membrane domain, Protein-lipid interaction, Self-assembly",
author = "Kaiser, {Hermann Josef} and Adam Orłowski and Tomasz R{\'o}g and Nyholm, {Thomas K.M.} and Wengang Chai and Ten Feizi and Daniel Lingwood and Ilpo Vattulainen and Kai Simons",
year = "2011",
month = "10",
day = "4",
doi = "10.1073/pnas.1103742108",
language = "English",
volume = "108",
pages = "16628--16633",
journal = "Proceedings of the National Academy of Sciences",
issn = "0027-8424",
number = "40",

}

RIS - Download

TY - JOUR

T1 - Lateral sorting in model membranes by cholesterol-mediated hydrophobic matching

AU - Kaiser, Hermann Josef

AU - Orłowski, Adam

AU - Róg, Tomasz

AU - Nyholm, Thomas K.M.

AU - Chai, Wengang

AU - Feizi, Ten

AU - Lingwood, Daniel

AU - Vattulainen, Ilpo

AU - Simons, Kai

PY - 2011/10/4

Y1 - 2011/10/4

N2 - 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.

AB - 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.

KW - Annular lipid

KW - Mattress model

KW - Membrane domain

KW - Protein-lipid interaction

KW - Self-assembly

UR - http://www.scopus.com/inward/record.url?scp=80053632190&partnerID=8YFLogxK

U2 - 10.1073/pnas.1103742108

DO - 10.1073/pnas.1103742108

M3 - Article

VL - 108

SP - 16628

EP - 16633

JO - Proceedings of the National Academy of Sciences

JF - Proceedings of the National Academy of Sciences

SN - 0027-8424

IS - 40

ER -

ID: 17001272