ZnO film based surface acoustic wave micro-pump

In this study, a micro-pump unit based on surface acoustic wave (SAW) on piezoelectric ZnO film is designed and fabricated as a micro-fluidic device. It employs a mechanical wave, which is generated electrically using an aluminum interdigital transducer (IDT), and propagates on the surface of the ZnO film. The ZnO film was used in this study because it has a high electromechanical coefficient and an excellent bonding with various substrate materials, in particular silicon. The sputtering parameters for ZnO film deposition have been optimized, and the ZnO films with different thickness from 1 micron to 5.5 microns were prepared. The film properties have been characterized using different methods, such as scanning electron microscopy, X-ray diffraction and atomic force microscopy. Aluminum IDT with a finger width and spacing of 8 microns was patterned on the ZnO film using a lift-off process. The frequency generated was measured using a network analyzer, and it varies from 130 MHz to 180 MHz as a function of film thickness. A signal generator was used to generate the frequency with a power amplifier to amplify the signal, which was then applied to aluminum IDT to generate the surface acoustic wave. If a liquid droplet exists on the surface carrying the acoustic wave, the energy and the momentum of the SAW will be coupled into the fluid, causing the liquid to vibrate and move on film surface. The strength of this movement is determined by the applied voltage and frequency. The volume of the liquid drop loaded on the SAW device in this study is of several hundreds of nanoliters. The movement of the liquid inside the droplet and also on the ZnO film surface can be demonstrated. The performance of ZnO SAW device was characterized as a function of film thickness. © 2007 IOP Publishing Ltd.

Binding of the molecular chaperone αB-crystallin to Aβ amyloid fibrils inhibits fibril elongation.

The molecular chaperone αB-crystallin is a small heat-shock protein that is upregulated in response to a multitude of stress stimuli, and is found colocalized with Aβ amyloid fibrils in the extracellular plaques that are characteristic of Alzheimer's disease. We investigated whether this archetypical small heat-shock protein has the ability to interact with Aβ fibrils in vitro. We find that αB-crystallin binds to wild-type Aβ(42) fibrils with micromolar affinity, and also binds to fibrils formed from the E22G Arctic mutation of Aβ(42). Immunoelectron microscopy confirms that binding occurs along the entire length and ends of the fibrils. Investigations into the effect of αB-crystallin on the seeded growth of Aβ fibrils, both in solution and on the surface of a quartz crystal microbalance biosensor, reveal that the binding of αB-crystallin to seed fibrils strongly inhibits their elongation. Because the lag phase in sigmoidal fibril assembly kinetics is dominated by elongation and fragmentation rates, the chaperone mechanism identified here represents a highly effective means to inhibit fibril proliferation. Together with previous observations of αB-crystallin interaction with α-synuclein and insulin fibrils, the results suggest that this mechanism is a generic means of providing molecular chaperone protection against amyloid fibril formation.