Hydration layers are formed on hydrophilic crystalline surfaces immersed in water.

The structure and the role of the interfacial water in mediating the interactions of extended hydrophobic surfaces are not well understood. Two-dimensional materials provide a variety of large and atomically flat hydrophobic surfaces to facilitate our understanding of hydrophobic interactions. The angstrom resolution capabilities of three-dimensional AFM are exploited to image the interfacial water organization on graphene, few-layer MoS 2 and few-layer WSe 2 . Those interfaces are characterized by the existence of a 2 nm thick region above the solid surface where the liquid density oscillates. The distances between adjacent layers for graphene, few-layer MoS 2 and WSe 2 are ~0.50 nm. This value is larger than the one predicted and measured for water density oscillations (~0.30 nm). The experiments indicate that on extended hydrophobic surfaces water molecules are expelled from the vicinity of the surface and replaced by several molecular-size hydrophobic layers.

Capillary condensation of water from vapor is an everyday phenomenon which has a wide range of scientific and technological implications. Many aspects of capillary condensation are not well understood such as the structure of interfacial water, the existence of distinct properties of confined water, or the validity of the Kelvin equation at nanoscale. We note the absence of high-spatial resolution images inside a meniscus. Here, we develop an AFM-based method to provide in situ atomic-scale resolution maps of the solid–water interface of a nanomeniscus (80–250 nm 3 ). The separation between the first two hydration layers on graphite is 0.30 nm, while on mica it is 0.28 nm. Those values are very close to the ones expected for the same surfaces immersed in bulk water. Thus, the hydration layer structure on a crystalline surface is independent of the water volume.

The mechanical properties of collagen fibrils depend on the amount and the distribution of water molecules within the fibrils. Here, we use atomic force microscopy (AFM) to study the effect of hydration on the viscoelastic properties of reconstituted type I collagen fibrils in air with controlled relative humidity. With the same AFM tip, we investigate the same area of a collagen fibril with two different force spectroscopy methods: force-distance (FD) and amplitude-phase-distance (APD) measurements. This allows us to separate the contributions of the fibril's viscoelastic response and the capillary force to the tip-sample interaction. A water bridge forms between the tip apex and the surface, causing an attractive capillary force, which is the main contribution to the energy dissipated from the tip to the specimen in dynamic AFM. The force hysteresis in the FD measurements and the tip indentation of only 2 nm in the APD measurements show that the hydrated collagen fibril is a viscoelastic solid. The mechanical properties of the gap regions and the overlap regions in the fibril's D-band pattern differ only in the top 2 nm but not in the fibril's bulk. We attribute this to the reduced number of intermolecular crosslinks in the reconstituted collagen fibril. The presented methodology allows the mechanical surface properties of hydrated collagenous tissues and biomaterials to be studied with unprecedented detail on the nanometer scale.

High-speed AFM enabled the imaging of protein interactions with millisecond time resolutions (10 fps). However, the acquisition of nanomechanical maps of proteins is about 100 times slower. Here, we developed a high-speed bimodal AFM that provided high-spatial resolution maps of the elastic modulus, the loss tangent and the topography at imaging rates of 5.7 fps. The new microscope was applied to identify the initial stages of the self-assembly of the collagen structures. By following the changes in the physical properties we identified four stages, nucleation and growth of collagen precursors, formation of tropocollagen molecules, assembly of tropocollagens into microfibrils, and alignment of microfibrils to generate microribbons. Some emerging collagen structures never matured and, after an existence of several seconds, they disappeared into the solution. The elastic modulus of a microfibril (~4 MPa) implied very small stiffness (~3x10 -6 N/m). Those values amplified the amplitude of the collagen thermal fluctuations on the mica plane which facilitated microribbon built-up.