Effects of a Hydrophilic/Hydrophobic Interface on Amyloid-β Peptides Studied by Molecular Dynamics Simulations and NMR Experiments

Oligomer formation of amyloid-β peptides (Aβ) is accelerated at a hydrophilic/hydrophobic interface. However, details of the acceleration mechanism have not been elucidated. To understand the effects of the interface on oligomerization at the atomic level, we performed molecular dynamics simulations for an Aβ40 monomer in the presence and absence of the hydrophilic/hydrophobic interface. Nuclear magnetic resonance experiments of Aβ40 peptides...