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 ... VO - 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 N1 - PP - ER -