Superhydrophobic Surface by Laser Ablation of PDMS.

Superhydrophobic surfaces have important applications in generating anti-icing properties, preventing corrosion, producing anti-biofouling characteristics, and microfluidic devices. One of the most commonly used materials to make superhydrophobic surfaces is poly(dimethylsiloxane) (PDMS). Various techniques, including spin-coating, dip-coating, spray coating, surface etching, and laser-textured mold methods, have been used to make superhydrophobic surfaces. However, all these methods require several steps, the usage of multiple chemicals, and/or surface modifications. In this paper, a one-step, low-cost method to induce superhydrophobicity is described. This was done by the pulsed laser deposition of laser-ablated PDMS micro/nanoparticles, and the method applies to a variety of surfaces. This technique has been demonstrated on three important classes of material─glass, poly(methyl methacrylate) (PMMA), and aluminum. Water contact angles of greater than 150° and roll-off angles of less than 3° were obtained. Optical transmission value of as high as 90% was obtained on glass or PMMA coated with laser-ablated PDMS micro/nanoparticles. Furthermore, this method can also be used to make micron-scale patterned superhydrophobic PDMS surfaces. This would have potential applications in microfluidic microchannels and other optical devices.

Capturing the Polarization Response of Solvated Proteins under Constant Electric Fields in Molecular Dynamics Simulations.

We capture and compare the polarization response of a solvated globular protein ubiquitin to static electric (E-fields) using atomistic molecular dynamics simulations. We collectively follow E-field induced changes, electrical and structural, occurring across multiple trajectories using the magnitude of the protein dipole vector (Pp ). E-fields antiparallel to Pp induce faster structural changes and more facile protein unfolding relative to parallel fields of the same strength. While weak E-fields (0.1-0.5 V/nm) do not unfold ubiquitin and produce a reversible polarization, strong E-fields (1-2 V/nm) unfold the protein through a pathway wherein the helix:ß-strand interactions rupture before those for the ß1-ß5 clamp. Independent of E-field direction, high E-field induced structural changes are also reversible if the field is switched off before Pp exceeds 2 times its equilibrium value. We critically examine the dependence of water properties, protein rotational diffusion and E-field induced protein unfolding pathways on the thermostat/barostat parameters used in our simulations.