Molecular dynamics simulation studies of the structural response of an isolated Aβ1-42 monomer localized in the vicinity of the hydrophilic TiO 2 surface.

We have probed the effect of a model hydrophilic surface, rutile TiO(2), on the full-length amyloid beta (Aβ(1-42)) monomer using molecular dynamics simulations. The rutile surface brings about sharp changes in the peptide's intrinsic behavior in a distance-dependent manner. The intrinsic collapse of the peptide is disrupted, while the β-sheet propensity is sharply enhanced with increased proximity to the surface. The results may have implications for Aβ self-assembly and fibrillogenesis on hydrophilic surfaces and should be taken into consideration in the design of novel nanomaterials for perturbing amyloidogenic behavior.