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Distance synergy of MoS2-confined Rh atoms for highly efficient hydrogen evolution.

Perturbing the electronic structure of MoS2 basal plane via confining heteroatoms offers the opportunity to trigger in-plane activity for hydrogen evolution reaction (HER). The key challenge consists in inducing the optimum HER activity by controlling the type and distribution of confined atoms. Herein, we report a distance synergy of MoS2-confined single-atom rhodium realizing an ultra-high HER activity at the in-plane S sites adjacent to the rhodium. By optimizing the distance between the confined Rh atoms, an ultra-low overpotential of 67 mV is achieved at a current density of 10 mA cm-2 in acidic solution. Experiments and first-principles calculations demonstrate a unique distance synergy between the confined rhodium atoms in tuning the reactivity of neighbouring in-plane S atoms, which presents a volcanic trend with the inter-rhodium distance. This study provides a new strategy to tailor the activity of MoS2 surface via modulating the distance between confined single atoms.

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Afadin regulates actomyosin organization through αE-catenin at adherens junctions.

Actomyosin-undercoated adherens junctions are critical for epithelial cell integrity and remodeling. Actomyosin associates with adherens junctions through αE-catenin complexed with β-catenin and E-cadherin in vivo; however, in vitro biochemical studies in solution showed that αE-catenin complexed with β-catenin binds to F-actin less efficiently than αE-catenin that is not complexed with β-catenin. Although a "catch-bond model" partly explains this inconsistency, the mechanism for this inconsistency between the in vivo and in vitro results remains elusive. We herein demonstrate that afadin binds to αE-catenin complexed with β-catenin and enhances its F-actin-binding activity in a novel mechanism, eventually inducing the proper actomyosin organization through αE-catenin complexed with β-catenin and E-cadherin at adherens junctions.

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Alamandine attenuates hepatic fibrosis by regulating autophagy induced by NOX4-dependent ROS.

Angiotensin II (Ang II) has been reported to aggravate hepatic fibrosis by inducing NADPH oxidase (NOX)-dependent oxidative stress. Alamandine protects against fibrosis by counteracting Ang II via the MrgD receptor, though the effects of alamandine on hepatic fibrosis remain unknown. Autophagy activated by reactive oxygen species (ROS) is a novel mechanism of hepatic fibrosis. However, whether autophagy is involved in the regulation of Ang II-induced hepatic fibrosis still requires investigation. We explored the effect of alamandine on hepatic fibrosis via regulation of autophagy by redox balance modulation. In vivo, alamandine reduced ccl4-induced hepatic fibrosis, H2O2 content, protein levels of NOX4 and autophagy impairment. In vitro, Ang II treatment elevated NOX4 protein expression and ROS production along with upregulation of the ACE/Ang II/AT1R axis. These changes resulted in the accumulation of impaired autophagosomes in hepatic stellate cells (HSCs). Treatment withtheNOX4 inhibitor VAS2870, ROS scavenger N-acetylcysteine, and NOX4 small interfering RNA (siRNA) inhibited Ang II-induced autophagy and collagen synthesis. Alamandine shifted the balance of RAS toward the ACE2/alamandine/MrgD axis, and inhibited both Ang II-induced ROS and autophagy activation, leading to attenuation of HSCs migration or collagen synthesis. In summary, alamandine attenuated liver fibrosis by regulating autophagy induced by NOX4-dependent ROS.

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The ACE2 expression in human heart indicates new potential mechanism of heart injury among patients infected with SARS-CoV-2.

A new type of pneumonia caused by a novel coronavirus SARS-CoV-2 outbreaks recently in China and spreads into many other countries. This disease, named as COVID-19, is similar to patients infected by SARS-CoV and MERS-CoV, and nearly 20% of patients developed severe condition. Cardiac injury is a prevalent complication of severe patients, exacerbating the disease severity in coronavirus disease 2019 (COVID-19) patients. Angiotensin-converting enzyme 2 (ACE2), the key host cellular receptor of SARS-CoV-2, has been identified in multiple organs, but its cellular distribution in human heart is not illuminated clearly. This study performed the first state-of-art single cell atlas of adult human heart, and revealed that pericytes with high expression of ACE2 might act as the target cardiac cell of SARS-CoV-2. The pericytes injury due to virus infection may result in capillary endothelial cells dysfunction, inducing microvascular dysfunction. And patients with basic heart failure disease showed increased ACE2 expression at both mRNA and protein levels, meaning that if infected by the virus these patients may have higher risk of heart attack and critically ill condition. The finding of this study explains the high rate of severe cases among COVID-19 patients with basic cardiovascular disease; and these results also perhaps provide important reference to clinical treatment of cardiac injury among severe patients infected by SARS-CoV-2.

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Contact lens-based lysozyme detection in tear using a mobile sensor.

We report a method for sensing analytes in tear-fluid using commercial contact lenses (CLs) as sample collectors for subsequent analysis with a cost-effective and field-portable reader. In this study we quantify lysozyme, the most prevalent protein in tear fluid, non-specifically bound to CLs worn by human participants. Our mobile reader uses time-lapse imaging to capture an increasing fluorescent signal in a standard well-plate, the rate-of-change of which is used to indirectly infer lysozyme concentration through the use of a standard curve. We empirically determined the best-suited CL material for our sampling procedure and assay, and subsequently monitored the lysozyme levels of nine healthy human participants over a two-week period. Of these participants who were regular CL wearers (6 out of 9), we observed an increase in lysozyme levels from 6.89 ± 2.02 μg mL-1 to 10.72 ± 3.22 μg mL-1 (mean ± SD) when inducing an instance of digital eye-strain by asking them to play a game on their mobile-phones during the CL wear-duration. We also observed a lower mean lysozyme concentration (2.43 ± 1.66 μg mL-1) in a patient cohort with dry eye disease (DED) as compared to the average monitoring level of healthy (no DED) human participants (6.89 ± 2.02 μg mL-1). Taken together, this study demonstrates tear-fluid analysis with simple and non-invasive sampling steps along with a rapid, easy-to-use, and cost-effective measurement system, ultimately indicating physiological differences in human participants. We believe this method could be used in future tear-fluid studies, even supporting multiplexed detection of a panel of tear biomarkers toward improved diagnostics and prognostics as well as personalized mobile-health applications.

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Inducing secondary structural interplays between scallop muscle proteins and soy proteins to form soluble composites.

Developing food protein structures with the freedom to tune their internal molecular arrangements is a fascinating aspect for serving the demands of multifunctional food components. However, a protein's conformation is highly submissive to its amino acid sequences, posing a great limitation on controlling its structural rearrangements. In this study, based on simply co-dissolving scallop muscle proteins (SMPs, water-insoluble) and soya proteins (SPs) at pH 12 prior to neutralization, the unfolding-folding pathways of both proteins were altered. Structural characterizations evidenced the complexation of SMPs and SPs using their secondary structures as the building blocks. Due to hydrophobic coalition between the α-helix (from SMPs) and β-sheet (from SPs), the co-assembled structures obtained considerable resistance against folding triggered by the hydrophobic effect. In addition, the kinetics by which the SMPs and SPs folded together was tailor-made by the compositional differences of the two proteins, resulting in the formation of well-defined, water-dispersible nanospheres with a tunable size and internal arrangements of the backbones. This study would enrich our choice of manipulated protein structures and enlarge the available protein sources with tailorable functions when applied in specific scenarios.

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