Direct and simultaneous measurements of the normal and lateral forces encountered by a nanosize spherical silicon tip approaching a solid surface in purified water are reported. For tip-surface distances, 0 ± 0.03 nm Ͻ d Ͻ 2 nm, experiments and grand canonical molecular-dynamics simulations find oscillatory solvation forces for hydrophilic surfaces, mica and glass, and less pronounced oscillations for a hydrophobic surface, graphite. The simulations reveal layering of the confined water density and the development of hexagonal order in layers proximal to a quartz surface. For subnanometer hydrophilic confinement, the lateral force measurements show orders of magnitude increase of the viscosity with respect to bulk water, agreeing with a simulated sharp decrease in the diffusion constant. No viscosity increase is observed for hydrophobic surfaces.

We report a nanolithography technique that allows simultaneous direct control of the local chemistry and topography of thin polymer films. Specifically, a heated atomic force microscope (AFM) tip can write sub-15 nm hydrophilic features onto a hydrophobic polymer at the rate of 1.4 mm per s. The thermally activated chemical reactions and topography changes depend on the chemical composition of the polymer, the raster speed, the temperature at the AFM tip/sample interface, and the normal load. This method is conceptually simple, direct, extremely rapid, achievable in a range of environments, and potentially adaptable to other materials systems.

The effect of mechanical force on the free-energy surface that governs a chemical reaction is largely unknown. The combination of protein engineering with single-molecule force-clamp spectroscopy allows us to study the influence of mechanical force on the rate at which a protein disulfide bond is reduced by nucleophiles in a bimolecular substitution reaction (S(N)2). We found that cleavage of a protein disulfide bond by hydroxide anions exhibits an abrupt reactivity 'switch' at ∼500 pN, after which the accelerating effect of force on the rate of an S(N)2 chemical reaction greatly diminishes. We propose that an abrupt force-induced conformational change of the protein disulfide bond shifts its ground state, drastically changing its reactivity in S(N)2 chemical reactions. Our experiments directly demonstrate the action of a force-activated switch in the chemical reactivity of a single molecule.

Water bridges formed through capillary condensation at nanoscale contacts first stretch and then break during contact rupture. Atomic force microscopy (AFM) pull-off experiments performed in air with hydrophilic tips and samples show that stretched nanoscopic water bridges are in mechanical equilibrium with the external pull-off force acting at the contact but not in thermodynamic equilibrium with the water vapor in air. The experimental findings are explained by a theoretical model that considers constant water volume and decrease of water meniscus curvature during meniscus stretching. The model predicts that the water bridge breakup distance will be roughly equal to the cubic root of the water bridge volume. A thermodynamic instability was noticed for large water bridges formed at the contact of a blunt AFM tip (curvature radius of 400 nm) with a flat sample. In this case, experiments showed rise and stabilization of the volume of the water at the contact in about 1 s. For sharp AFM tips (curvature radius below 50 nm), the experiments indicated that formation of stable water bridges occurs in a much shorter time (below 5 ms).