4.1. MD simulations protocol

The all‐atom MD simulations were preformed using the GROMACS‐5.1.4 package. ⁷⁷ The all‐atom CHARMM36‐2015 force‐field for GROMACS ⁷⁸ was applied to describe the Aβ peptides, lipids, ions, and TIP3P water model. ⁷⁹ Each system was first energy minimized by using steepest decent algorithm and then was equilibrated in two phases. Throughout the equilibration, position restrains were applied to all peptides' heavy atoms (i.e., nonhydrogen) with force constant of 1,000 kJ mol⁻¹ nm⁻² in order to adjust the peptides' atoms to lipids and water molecules. In the first phase, the equilibration lasted for 10 ns under isothermal‐isochoric (NVT) conditions by velocity‐rescale thermostat ⁸⁰ with coupling constant of 0.1 ps to regulate separately the temperature of 310 K for peptides, lipids, and solvent (including ions). In the second phase, the systems were equilibrated over 50 ns under isothermal‐isobaric (NPT) conditions by using the Nose–Hoover thermostat ^{81 , 82} to regulate the temperature, along with semi‐isotropic Parrinello–Rahman pressure coupling scheme, ^{83 , 84} to obtain pressure of 1 bar in the x–y plane and the normal z‐direction with time constant of 5 ps. Then to equilibration, MD simulations were performed for 700 ns for each system; thus, a total of 2.8 μs has been performed in this work. In this step, the NPT ensemble was used, in the absence of restraints. In the simulations, LINCS algorithm was used to constrain bonds involving hydrogen. ⁸⁵ Electrostatic interactions were calculated using the particle mesh Ewald method ^{86 , 87} with cutoff of 1.2 Å, and van der Waals interactions used a cutoff of 12 Å. A time step of 2 fs was used for integration, while the coordinates and velocities were saved every 20 ps for analysis. Periodic boundary conditions were set in all directions.