TY  -  
T1  - Physiologically-relevant levels of sphingomyelin, but not GM1, induces a beta-sheet-rich structure in the amyloid-beta(1-42) monomer 
SN  -  /  
UR  - http://hdl.handle.net/10138/300673 
T3  -  
A1  - Owen, Michael C.; Kulig, Waldemar; Poojari, Chetan; Rog, Tomasz; Strodel, Birgit 
A2  -  
PB  -  
Y1  - 2018 
LA  - eng 
AB  - 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 ... 
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IS  -  
SP  -  
OP  -  
KW  - Peptide-membrane interactions; Sphingomyelin; Lipid rafts; Amyloid-β peptide; Molecular dynamics; Membrane simulations; GM1; Gangliosides; Peptide-ganglioside interactions; MEMBRANE DISRUPTION; MOLECULAR-DYNAMICS; FIBRIL STRUCTURE; ALZHEIMERS-DISEASE; PEPTIDE; AMYLOID-BETA; Amyloid-beta peptide; A-BETA; FORCE-FIELD; PHOSPHOLIPID-BILAYERS; LIPID-BILAYER; 1182 Biochemistry, cell and molecular biology 
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ER  -