File S1 - Stability of Transmembrane Amyloid β-Peptide and Membrane Integrity Tested by Molecular Modeling of Site-Specific Aβ42 Mutations

Contains: Figure S1 Secondary structure analysis for the 500 ns MD simulations of WT Aβ42 as (a) β-sheet monomer and (b) β-sheet tetramer in a POPC bilayer. Figure S2 Secondary structure analysis for the 500 ns MD simulations of mutant Aβ42 monomer as (a) E22G, (b) D23G in a POPC bilayer. Figure S3 Secondary structure analysis for the 500 ns MD simulations of mutant Aβ42 monomer as (a) E22G/D23G, (b) K16M/K28M, (c) K16M/E22G/D23G/K28M in a POPC bilayer. Figure S4 Secondary structure analysis for the 500 ns MD simulation of E22G Aβ42 tetramer in a POPC bilayer. Figure S5 Secondary structure analysis for the 500 ns MD simulation of D23G Aβ42 tetramer in a POPC bilayer. Figure S6 Minimum distance between the anionic carboxylate of D23 and the cationic ammonium from K28 in the WT monomer and the E22G tetramer. Figure S7 Peptide-lipid interactions for the E22G monomer decomposed into Coulomb and Lennard-Jones interactions. Figure S8 Bilayer phosphate-to-phosphate thickness, averaged over the last 400 ns of the 500 ns MD simulations of WT Aβ42 as (a) β-sheet monomer and (b) β-sheet tetramer in a POPC bilayer. Figure S9 Bilayer phosphate-to-phosphate thickness, averaged over last 400 ns of the 500 ns MD simulations of Aβ mutants (monomers and tetramers). Figure S10 Time-averaged order parameter SCD of the palmitoyl chain of the POPC lipids. Results are shown for WT, E22G and D23G Aβ42 monomer. Figure S11 Time-averaged order parameter SCD of the palmitoyl chain of the POPC lipids. Results are shown for WT, E22G/D23G, K16M/K28M and K16M/E22G/D23G/K28M Aβ42 monomer. Figure S12 Time-averaged order parameter SCD of the palmitoyl chain of the POPC lipids. Results are shown for WT, E22G and D23G Aβ42 tetramer. (PDF)