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| Home > Publications database > Physiologically-relevant levels of sphingomyelin, but not GM1, induces a β-sheet-rich structure in the amyloid-β(1-42) monomer > print |
| 001 | 858916 | ||
| 005 | 20210130000134.0 | ||
| 024 | 7 | _ | |a 10.1016/j.bbamem.2018.03.026 |2 doi |
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| 100 | 1 | _ | |a Owen, Michael C. |0 P:(DE-HGF)0 |b 0 |
| 245 | _ | _ | |a Physiologically-relevant levels of sphingomyelin, but not GM1, induces a β-sheet-rich structure in the amyloid-β(1-42) monomer |
| 260 | _ | _ | |a Amsterdam |c 2018 |b Elsevier |
| 336 | 7 | _ | |a article |2 DRIVER |
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| 336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
| 520 | _ | _ | |a To resolve the contribution of ceramide-containing lipids to the aggregation of the amyloid-β protein into β-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 Aβ42 (and also residues Ser26, Asn27, and Lys28), which facilitated the formation of a β-sheet in the normally disordered N-terminal region. Aβ42 remained anchored to the SM-enriched bilayer through hydrogen bonds with the side chain of Arg5. With β-sheets in the at the N and C termini, the structure of Aβ42 in the sphingomyelin-enriched bilayer most resembles β-sheet-rich structures found in higher-ordered Aβ fibrils. Conversely, when bound to a bilayer comprised of 5% GM1, the conformation remained similar to that observed in the absence of GM1, with Aβ42 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. |
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| 700 | 1 | _ | |a Rog, Tomasz |0 P:(DE-HGF)0 |b 3 |
| 700 | 1 | _ | |a Strodel, Birgit |0 P:(DE-Juel1)132024 |b 4 |e Corresponding author |u fzj |
| 773 | _ | _ | |a 10.1016/j.bbamem.2018.03.026 |g Vol. 1860, no. 9, p. 1709 - 1720 |0 PERI:(DE-600)2209384-9 |n 9 |p 1709 - 1720 |t Biochimica et biophysica acta / Biomembranes Biomembranes [...] |v 1860 |y 2018 |x 0005-2736 |
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