title: Molecular dynamics simulation studies of the structural response of an isolated Aβ1-42 monomer localized in the vicinity of the hydrophilic TiO 2 surface.
abstract: 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.
authors.affiliation: Physical Chemistry Division, CSIR-National Chemical Laboratory, Pune, 411008, India.
authors.forename: Jaya C
authors.initials: JC
authors.lastname: Jose
authors.forename: Neelanjana
authors.initials: N
authors.lastname: Sengupta
mesh_terms: D016229:Amyloid beta-Peptides / Q000737:chemistry*; D057927:Hydrophobic and Hydrophilic Interactions; D008958:Models, Molecular; D056004:Molecular Dynamics Simulation; D049329:Nanostructures / Q000737:chemistry; D010446:Peptide Fragments / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry; D011487:Protein Conformation; D025941:Protein Interaction Mapping; D017433:Protein Structure, Secondary; D013499:Surface Properties; D014025:Titanium / Q000737:chemistry*
chemical_list: D016229:Amyloid beta-Peptides; D010446:Peptide Fragments; D010455:Peptides; C075222:amyloid beta-protein (1-42); C009495:titanium dioxide; D014025:Titanium