A small scroll expander has been incorporated into a power cycle for performance evaluation. Using heat from a circulating hot oil supply, a working fluid (R123) was vapourized under pressure and fed to the inlet of the expander. Power generated was measured by a torque/rotation rate sensor as the power was delivered to a compressor. The exhausted working fluid was then sent through a regenerator to recover thermal energy, and then to an air-cooled condensation heat exchanger. To complete the cycle, the working fluid passed through a pump and was fed back to the boiler by way of the regenerator. The major components of the power cycle were monitored for performance, and from these values, overall cycle efficiency was determined. A model of the system was also developed in order to validate system state points and allow follow-on projections of cycle performance with better component efficiencies. Depending on the operating state points during testing, the power output from the cycle ranged from 187 to 256 W. At nominal ambient outside temperatures (22.5 °C), the system efficiency was 7.2 per cent. The critical component limiting the overall system efficiency was the expander. Operating within the power cycle, expander efficiency was measured at levels between 45 and 50 per cent, based on the isentropic ideal. The obvious path forward is to improve the efficiency of the scroll expander.

A small-scale scroll expander was developed and tested. The expander was based on a compliant scroll compressor having a displacement of ∼6.8 cm3. A test loop was also developed for determining expander performance parameters. The loop employed a compressor to pressurize the working fluid up to 2758 kPa and a heat exchanger to create the expander inlet conditions that would characterize an operating power cycle. The expander was tested with R134a as the working fluid. For power output measurements, a dynamometer was used where torque and rotational rate were measured. An important feature in adapting a scroll compressor to expander duty was the lubrication of the scroll wraps during operation and the lubrication required by the journal bearings within the expander housing. The approach used in this study was to dissolve a compatible oil into the circulating working fluid to lubricate the wraps, while a pump was employed to deliver pressurized oil to the bearings. The pressurized oil supply was also used to generate a controlled force to the upper stationary scroll wrap through a sealed piston assembly. This force maintained axial contact between the upper and lower scroll wraps during operation. After expansion, the R134a vapour passed through an orifice flow meter and then to a liquid-cooled heat exchanger. It then enters a compressor and heat exchanger to complete the flow loop. A series of performance tests were conducted on the expander at various expander rotational speeds, inlet and outlet pressures, and scroll sealing pressures. Test results show consistent isentropic efficiencies of over 70 per cent for the expander at its maximum efficiency operating points. The expander performance, however, is a function of speed, pressure ratio, and scroll sealing pressure.

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K777 is a di-peptide analog that contains an electrophilic vinyl-sulfone moiety and is a potent, covalent inactivator of cathepsins. Vero E6, HeLa/ACE2, Caco-2, A549/ACE2, and Calu-3, cells were exposed to SARS-CoV-2, and then treated with K777. K777 reduced viral infectivity with EC50 values of inhibition of viral infection of: 74 nM for Vero E6, <80 nM for A549/ACE2, and 4 nM for HeLa/ACE2 cells. In contrast, Calu-3 and Caco-2 cells had EC50 values in the low micromolar range. No toxicity of K777 was observed for any of the host cells at 10-100 μM inhibitor. K777 did not inhibit activity of the papain-like cysteine protease and 3CL cysteine protease, encoded by SARS-CoV-2 at concentrations of ≤ 100 μM. These results suggested that K777 exerts its potent anti-viral activity by inactivation of mammalian cysteine proteases which are essential to viral infectivity. Using a propargyl derivative of K777 as an activity-based probe, K777 selectively targeted cathepsin B and cathepsin L in Vero E6 cells. However only cathepsin L cleaved the SARS-CoV-2 spike protein and K777 blocked this proteolysis. The site of spike protein cleavage by cathepsin L was in the S1 domain of SARS-CoV-2 , differing from the cleavage site observed in the SARS CoV-1 spike protein. These data support the hypothesis that the antiviral activity of K777 is mediated through inhibition of the activity of host cathepsin L and subsequent loss of viral spike protein processing.

Bubble nucleation control, growth and departure dynamics is important in understanding boiling phenomena and enhancing nucleate boiling heat transfer performance. We report a novel bi-functional heterogeneous surface structure that is capable of tuning bubble nucleation, growth and departure dynamics. For the fabrication of the surface, hydrophobic polymer dot arrays are first printed on a substrate, followed by hydrophilic ZnO nanostructure deposition via microreactor-assisted nanomaterial deposition (MAND) processing. Wettability contrast between the hydrophobic polymer dot arrays and aqueous ZnO solution allows for the fabrication of heterogeneous surfaces with distinct wettability regions. Heterogeneous surfaces with various configurations were fabricated and their bubble dynamics were examined at elevated heat flux, revealing various nucleate boiling phenomena. In particular, aligned and patterned bubbles with a tunable departure frequency and diameter were demonstrated in a boiling experiment for the first time. Taking advantage of our fabrication method, a 6 inch wafer size heterogeneous surface was prepared. Pool boiling experiments were also performed to demonstrate a heat flux enhancement up to 3X at the same surface superheat using bi-functional surfaces, compared to a bare stainless steel surface.

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