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@article{1506977,
author = {Owen, Michael Christopher and Kulig, W. and Poojari, C. and Rog, T. and Strodel, B.},
article_location = {AMSTERDAM},
article_number = {9},
doi = {http://dx.doi.org/10.1016/j.bbamem.2018.03.026},
keywords = {Peptide-membrane interactions; Sphingomyelin; Lipid rafts; Amyloid-beta peptide; Molecular dynamics; Membrane simulations; GM1; Gangliosides; Peptide-ganglioside interactions},
language = {eng},
issn = {0005-2736},
journal = {BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES},
title = {Physiologically-relevant levels of sphingomyelin, but not GM1, induces a beta-sheet-rich structure in the amyloid-beta(1-42) monomer},
volume = {1860},
year = {2018}
}
TY - JOUR
ID - 1506977
AU - Owen, Michael Christopher - Kulig, W. - Poojari, C. - Rog, T. - Strodel, B.
PY - 2018
TI - Physiologically-relevant levels of sphingomyelin, but not GM1, induces a beta-sheet-rich structure in the amyloid-beta(1-42) monomer
JF - BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
VL - 1860
IS - 9
SP - 1709-1720
EP - 1709-1720
PB - ELSEVIER SCIENCE BV
SN - 00052736
KW - Peptide-membrane interactions
KW - Sphingomyelin
KW - Lipid rafts
KW - Amyloid-beta peptide
KW - Molecular dynamics
KW - Membrane simulations
KW - GM1
KW - Gangliosides
KW - Peptide-ganglioside interactions
N2 - To resolve the contribution of ceramide-containing lipids to the aggregation of the amyloid-beta protein into beta sheet rich toxic oligomers, we employed molecular dynamics simulations to study the effect of cholesterol containing bilayers comprised of POPC (70% POPC, and 30% cholesterol) and physiologically relevant concentrations of sphingomyelin (SM) (30% SM, 40% POPC, and 30% cholesterol), and the GM1 ganglioside (5% GM1, 70% POPC, and 25% cholesterol). The increased bilayer rigidity provided by SM (and to a lesser degree, GM1) reduced the interactions between the SM-enriched bilayer and the N-terminus of A beta 42 (and also residues Ser26, Asn27, and Lys28), which facilitated the formation of a beta-sheet in the normally disordered N-terminal region. A beta 42 remained anchored to the SM-enriched bilayer through hydrogen bonds with the side chain of Arg5. With beta-sheets in the at the N and C termini, the structure of A beta 42 in the sphingomyelin-enriched bilayer most resembles beta-sheet-rich structures found in higher-ordered All fibrils. Conversely, when bound to a bilayer comprised of 5% GM1, the conformation remained similar to that observed in the absence of GM1, with A beta 42 only making contact with one or two GM1 molecules. This article is part of a Special Issue entitled: Protein Aggregation and Misfolding at the Cell Membrane Interface edited by Ayyalusamy Ramamoorthy.
ER -
OWEN, Michael Christopher, W. KULIG, C. POOJARI, T. ROG a B. STRODEL. Physiologically-relevant levels of sphingomyelin, but not GM1, induces a beta-sheet-rich structure in the amyloid-beta(1-42) monomer. \textit{BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES}. AMSTERDAM: ELSEVIER SCIENCE BV, 2018, roč.~1860, č.~9, s.~1709-1720. ISSN~0005-2736. Dostupné z: https://dx.doi.org/10.1016/j.bbamem.2018.03.026.
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