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Graphene oxide (GO) membranes, known for their high dielectric constant and low dielectric loss, have emerged as promising separators for advanced energy storage and transfer devices. While previous research has focused on the aqueous stability enhancement by high-valence metal cations, their effect on modifying the dielectric properties of GO membranes remains understudied. This study investigates the impact of transition metal cation modification on the aqueous stability and dielectric properties of graphene oxide (GO) membranes. Multivalent transition metal chlorides (FeCl3, FeCl2, CuCl2, and CuCl) were introduced during the self-assembly process to create modified GO membranes. The membranes were characterized using various techniques, including zeta potential measurements, contact angle measurements, FTIR spectroscopy, and XRD spectroscopy. The aqueous stability of the modified membranes was evaluated, and their dielectric performance was assessed using capacitance measurements across a frequency range of 0.1 Hz to 105 Hz. The results demonstrate that the choice of transition metal cation and its oxidation state significantly influence the morphology, aqueous stability, and dielectric properties of the GO membranes. Notably, Fe3+ and Cu2+ modifications enhanced aqueous stability, while Fe2+ and Cu+ modifications improved dielectric performance. This study provides insights into tailoring the properties of GO membranes for various applications, including energy storage and transfer devices. 

Abstract DNA–transcription factor (TF) interactions are essential for gene regulation. Fully characterizing TF recognition specificities and identifying their genomic binding targets are important to understand TF function and regulatory networks. Recently, high-throughput sequencing technology HT-SELEX (high-throughput systematic evolution of ligands by exponential enrichment) has been used to measure hundreds of TFs, providing massive datasets that comprise TF binding preferences. However, there is a need to develop comprehensive computational modeling to fully extract and characterize critical TF binding preferences and fail to distinguish genome-wide binding targets. In this study, we developed a global pairwise model called DCA-Scapes trained with experimental HT-SELEX data. Our approach uncovered high-resolution TF recognition specificity landscapes, enabled the prediction of in vivo binding sequences, and was validated with ChIP-seq (ChIP sequencing) data. In addition, the DCA-Scapes model was utilized to refine the locations of binding regions and accurately identify the binding sites within the ChIP-seq enriched peaks. Moreover, we extended our model to cover the entire human genome, uncovering potential TF target sites that exhibit tissue-specific TF recognition across various cellular environments. 

Developing low-cost and multiplexing electrochemical (EC) devices for bioassay is imperative. Herein, a polymer-based EC device, named EC 6-well plate, was proposed and fabricated using a non-photolithography method. Polyethylene terephthalate glycol (PETG) was used as a substrate and laser-cut polyester (PET) film was used as a mask for patterning the electrodes. The diameter of the working electrode (WE) was 900 μ m, and each WE-modifying step only requires 1 μ l of reagent. Acrylic mold with wells (60 μ l) was bonded to the PETG substrate. Miniaturization of reference electrodes (RE) was discussed. The solid-state Ag/AgCl RE-based three-electrode system, the Au three-electrode system (3E), and Au two-electrode system (2E) were prepared and employed to develop an immunosensor for toxin B detection. Differential pulse voltammetry (DPV) and electrochemical impedance spectroscopy (EIS) were applied to test the stability of the EC immunosensor. The solid-state Ag/AgCl RE-based system showed a standard deviation of open circuit potential (OCP) of 4.6 mV. The 3E system and 2E system showed the standard deviations of OCP of 0.0026 mV and 0.32 mV, respectively. It revealed that the EC 6-well plate with the 3E system is excellent for developing an EC immunosensor. 

The visualization of chloride in living cells with fluorescent sensors is linked to our ability to design hosts that can overcome the energetic penalty of desolvation to bind chloride in water. Fluorescent proteins can be used as biological supramolecular hosts to address this fundamental challenge. Here, we showcase the power of protein engineering to convert the fluorescent proton-pumping rhodopsin GR from Gloeobacter violaceus into GR1, a red-shifted, turn-on fluorescent sensor for chloride in detergent micelles and in live Escherichia coli . This non-natural function was unlocked by mutating D121, which serves as the counterion to the protonated retinylidene Schiff base chromophore. Substitution from aspartate to valine at this position (D121V) creates a binding site for chloride. The binding of chloride tunes the p K a of the chromophore towards the protonated, fluorescent state to generate a pH-dependent response. Moreover, ion pumping assays combined with bulk fluorescence and single-cell fluorescence microscopy experiments with E. coli , expressing a GR1 fusion with a cyan fluorescent protein, show that GR1 does not pump ions nor sense membrane potential but instead provides a reversible, ratiometric readout of changes in extracellular chloride at the membrane. This discovery sets the stage to use natural and laboratory-guided evolution to build a family of rhodopsin-based fluorescent chloride sensors with improved properties for cellular applications and learn how proteins can evolve and adapt to bind anions in water.