The thermal stability in structural and electrical properties of HfO 2 , HfAlO x alloy, and Al 2 O 3 /HfO 2 stack thin films prepared by atomic layer deposition were comparatively investigated. Both HfAlO x and Al 2 O 3 /HfO 2 exhibit improved property against thermal degradation compared to the HfO 2 film. However, the incorporation of Al in alloy form provides characteristics superior to that in stack structure by retaining an amorphous structure up to 1000°C, which suppresses the leakage current and retards the growth of interfacial layer giving rise to lower increment of equivalent-oxide-thickness and interface trap density.
The polymerization experiments were carried out in a calorimeter modified for UV irradiation [22]. The samples were prepared by adding 1 wt.-% photoinitiator, Irgacure 651 (Ciba-Geigy), and 200 ppm of inhibitor p-methoxyphenol to the monomer to avoid thermal polymerization (81.To prepare the polymer films, the monomers, provided with initiator and inhibitor, are pressed at 120-125°C between glass plates coated with polyimide. They are left at this temperature until a defect-free homeotropic alignment, with disks parallel to the substrate, is obtained (black films between crossed polarizers in optical microscopy). The films, from 4 to 15 pm thick, are then exposed to UV radiation for 15 min at varied polymerization temperatures. The resulting materials are defect-free, transparent and colorless.The ordinary (no) and extraordinary (n,) refractive indices of 2 and poIy(2) are measured with an Abbe refractometer. Wide-angle X-ray diffraction experiments were carried out on a Siemens Hi-Star Area Detector, using CuKa radiation.
SARS-CoV-2 infects humans through the binding of viral S-protein (spike protein) to human ACE2 (angiotensin I converting enzyme 2). The structure of the ACE2-S-protein complex has been deciphered and we focused on the 27 ACE2 residues that bind to S-protein. From human sequence databases, we identified 9 ACE2 variants at ACE2-S-protein binding sites. We used both experimental assays and protein structure analysis to evaluate the effect of each variant on the binding affinity of ACE2 to S-protein. We found one variant causing complete binding disruption, two and three variants, respectively, strongly and mildly reducing the binding affinity, and two variants strongly enhancing the binding affinity. We then collected the ACE2 gene sequences from 57 non-human primates. Among the six apes and 20 Old World monkeys (OWMs) studied we found no new variants. In contrast, all 11 New World monkeys (NWMs) studied share four variants each causing a strong reduction in binding affinity, the Philippine tarsier also possesses three such variants, and 18 of the 19 prosimian species studied share one variant causing a strong reduction in binding affinity. Moreover, one OWM and three prosimian variants increased binding affinity by > 50%. Based on these findings we proposed that the common ancestor of primates was strongly resistant to and that of NWMs was completely resistant to SARS-CoV-2 and so is the Philippine tarsier, whereas apes and OWMs, like most humans, are susceptible. This study increases our understanding of the differences in susceptibility to SARS-CoV-2 infection among primates.
The charge storage characteristics of metal-oxide-semiconductor structures containing Au nanocrystals in atomic-layer-deposited high-k gate dielectrics were studied. Cross-sectional high-resolution transmission electron microscopy reveals that the Au nanocrystals are self-assembled in the high-k dielectric matrix after high temperature annealing in N2 ambient. The memory effect was observed from capacitance-voltage (C-V) relations and a satisfactory charge retention characteristic was obtained in the sample using Al2O3 as the gate dielectric than in the one using Hf2AlOx. Moreover, a saturation of electron storage in the metal-oxide-semiconductor capacitors was also observed.
Entry inhibitors against severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) are urgently needed to control the outbreak of coronavirus disease 2019 (COVID-19). This study developed a robust and straightforward assay that detected the molecular interaction between the receptor-binding domain (RBD) of viral spike protein and the angiotensin-converting enzyme 2 (ACE2) receptor in just 10 min. A drug library of 1068 approved compounds was used to screen for SARS-CoV2 entry inhibition, and 9 active drugs were identified as specific pseudovirus entry inhibitors. A plaque reduction neutralization test using authentic SARS-CoV-2 virus in Vero E6 cells confirmed that 2 of these drugs (Etravirine and Dolutegravir) significantly inhibited the infection of SARS-CoV-2. With molecular docking, we showed that both Etravirine and Dolutegravir are preferentially bound to primary ACE2-interacting residues on the RBD domain, implying that these two drug blocks may prohibit the viral attachment of SARS-CoV-2. We compared the neutralizing activities of these entry inhibitors against different pseudoviruses carrying spike proteins from alpha, beta, gamma, and delta variants. Both Etravirine and Dolutegravir showed similar neutralizing activities against different variants, with EC50 values between 4.5 to 5.8 nM for Etravirine and 10.2 to 22.9 nM for Dolutegravir. These data implied that Etravirine and Dolutegravir may serve as general spike inhibitors against dominant viral variants of SARS-CoV-2.
The nonvolatile memory characteristics of metal-oxide-semiconductor (MOS) structures containing Au nanocrystals in the Al 2 O 3 /SiO 2 matrix were studied. In this work, we have demonstrated that the use of Al 2 O 3 as control oxide prepared by atomic-layer-deposition enhances the erase speed of the MOS capacitors. A giant capacitance-voltage hysteresis loop and a very short erase time which is lower than 1 ms can be obtained. Compared with the conventional floating-gate electrically erasable programmable read-only memories, the erase speed was promoted drastically. In addition, very low leakage current and large turnaround voltage resulting from electrons or holes stored in the Au nanocrystals were found in the current-voltage relation of the MOS capacitors.
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