Wetting and drying of hydrophobic pores with diameters lower than 0.2 μm by aqueous solutions at different hydrostatic pressures is investigated by measuring the ionic conductance variation through the nanopores. The critical pressure for water intrusion into the nanopores increases with lowering the pore diameter and the surface tension of the hydrophobic modification, in agreement with the Laplace equation. Nevertheless, restoring the pressure to the atmospheric one does not result in spontaneous pore dewetting unless bubbles are left inside the pores. Such bubbles can appear at the regions of narrowing cross section and/or varying quality of the hydrophobic modification and thus can be engineered to control water expulsion.
Nanoporous alumina membranes rendered hydrophobic by surface modification via covalent attachment of hydrocarbon or fluorocarbon chains conduct electricity via surface even when the pores are not filled with electrolyte. The resistance is many orders of magnitude higher than for electrolyte filled membranes and does not depend on the electrolyte concentration or pH but it does depend on the type of hydrophobic monolayer and its density. The corresponding surface resistance varies from greater than 10 18 Ω/□ to less than 3×10 9 Ω/□. When the hydrophobic monolayer contains a small proportion of photoactive spiropyran that is insufficient to switch the surface to hydrophilic after spiropyran photoisomerization to the merocyanine form, the membrane resistance also becomes light-dependent with a reversible increase of surface resistance by as much as 15%. Surface conduction is ascribed to hydration and ionization of the alumina surface hydroxyls and the ionizable groups of the hydrophobic surface modifiers.
A design of smart surfaces responsive to biochemical analytes is demonstrated in the example of mixed monolayers of biotin/fluorocarbon. The contact angle of aqueous solutions on such surfaces decreases upon streptavidin binding and can be used in detecting this protein. The specificity of the effect is confirmed by lack of the contact angle change by streptavidin blocked with biotin and by BSA.
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