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2D transition metal dichalcogenides are promising candidates for high‐performance photodetectors. However, the relatively low response speed as well as the complex transfer process hinders their wide applications. Herein, for the first time, the fabrication of a few‐layer MoTe2/Si 2D–3D vertical heterojunction for high‐speed and broadband photodiodes by a pulsed laser deposition technique is reported. Owing to the high junction quality, ultrathin MoTe2 film thickness, and unique vertical n–n heterojunction structure, the photodiode exhibits excellent device performance in terms of a high responsivity of 0.19 A W−1 and a large detectivity of 6.8 × 1013 Jones. The device is also capable of detecting a broadband light with wavelength spanning from 300 to 1800 nm. More importantly, the device possesses an ultrahigh response speed up to 150 ns with a 3‐dB electrical bandwidth approaching 0.12 GHz. This work paves the way toward the fabrication of novel 2D–3D heterojunctions for high‐performance, ultrafast photodetectors. [ABSTRACT FROM AUTHOR]

Generating stable antibodies is an important goal in the development of antibody-based drugs. Often, thermal stability is assumed predictive of overall stability. To test this, we used different internally created antibodies and first studied changes in antibody structure as a function of pH, using the dye ANS. Comparison of the pH50 values, the midpoint of the transition from the high-pH to the low-pH conformation, allowed us for the first time to rank antibodies based on their pH stability. Next, thermal stability was probed by heating the protein in the presence of the dye Sypro Orange. A new data analysis method allowed extraction of all three antibody unfolding transitions and showed close correspondence to values obtained by differential scanning calorimetry. T1%, the temperature at which 1% of the protein is unfolded, was also determined. Importantly, no correlations could be found between thermal stability and pH50, suggesting that to accurately quantify antibody stability, different measures of protein stability are necessary. The experimental data were further analyzed using a machine-learning approach with a trained model that allowed the prediction of biophysical stability using primary sequence alone. The pH stability predictions proved most successful and were accurate to within pH ±0.2. [ABSTRACT FROM AUTHOR]

LOX-1 is a scavenger receptor that functions as the primary receptor for oxidized low-density lipoprotein (OxLDL) in endothelial cells. The binding of OxLDL to LOX-1 is believed to lead to endothelial activation, dysfunction, and injury, which constitute early atherogenic events. Because of its potential pathological role in atherosclerosis, LOX-1 has been proposed as a therapeutic target for the treatment of this disease. In order to antagonize the ligand-binding function of cell surface LOX-1, we generated a series of recombinant human LOX-1–crystallizable fragment (Fc) fusion proteins and subsequently characterized their biochemical properties and ligand-binding activities in vitro. Consistent with the notion that oligomerization of cell surface LOX-1 is required for high-avidity binding of ligands, we found that LOX-1–Fc fusion protein containing four ligand-binding domains per Fc dimer, but not the one containing two ligand-binding domains, exhibited ligand-binding activity. Optimal ligand-binding activity could be achieved via crosslinking of LOX-1–Fc fusion proteins with a polyclonal antibody against Fc. The crosslinked LOX-1–Fc protein also effectively inhibited the binding and internalization of OxLDL by cell surface LOX-1. These findings demonstrate that functional oligomerization is required for recombinant LOX-1–Fc to function as an effective antagonist. Structured digital abstract • : LOX1 (uniprotkb: ) and LOX1 (uniprotkb: ) physically interact ( ) by molecular sieving ( ) [ABSTRACT FROM AUTHOR]