Common quasi-static electrostatic micro actuators have significant limitations in deflection due to electrode separation and unstable drive regions. State-of-the-art electrostatic actuators achieve maximum deflections of approximately one third of the electrode separation. Large electrode separation and high driving voltages are normally required to achieve large actuator movements. Here we report on an electrostatic actuator class, fabricated in a CMOS-compatible process, which allows high deflections with small electrode separation. The concept presented makes the huge electrostatic forces within nanometre small electrode separation accessible for large deflections. Electrostatic actuations that are larger than the electrode separation were measured. An analytical theory is compared with measurement and simulation results and enables closer understanding of these actuators. The scaling behaviour discussed indicates significant future improvement on actuator deflection. The presented driving concept enables the investigation and development of novel micro systems with a high potential for improved device and system performance.

The absorption coefficient of thick-films of the negative photoresist SU-8 is observed to be time dependent during photolithographic exposure by I-line ultraviolet light (λ=365nm); varying linearly from 38±1cm−1 to 49±1cm−1 for a surface exposure dose of 415mJ∕cm2. We develop a general model which enables the exposure dose to be calculated at a given photoresist depth for a given exposure time. We determine the critical exposure dose for the subsequent polymerization of SU-8 having an arbitrary thickness to be 49.4±3.9mJcm−2.

Protein stability and ligand-binding affinity measurements are widely required for the formulation of biopharmaceutical proteins, protein engineering and drug screening within life science research. Current techniques either consume too much of often precious biological or compound materials, in large sample volumes, or alternatively require chemical labeling with fluorescent tags to achieve measurements at submicrolitre volumes with less sample. Here we present a quantitative and accurate method for the determination of protein stability and the affinity for small molecules, at only 1.5-20 nL optical sample volumes without the need for fluorescent labeling, and that takes advantage of the intrinsic tryptophan fluorescence of most proteins. Coupled to appropriate microfluidic sample preparation methods, the sample requirements could thus be reduced 85,000-fold to just 10 8 molecules. The stability of wild-type FKBP-12 and a destabilizing binding-pocket mutant are studied in the presence and absence of rapamycin, to demonstrate the potential of the technique to both drug screening and protein engineering. The results show that 75% of the interaction energy between FKBP-12 and rapamycin originates from residue Phe99 in the binding site.