Synthesis of Porous BPPO-Based Anion Exchange Membranes for Acid Recovery Via Diffusion Dialysis

Diffusion dialysis (DD) is an anion exchange membrane-based functional separation process used for acid recovery. TMA (trimethylamine) and BPPO (brominated poly (2,6-dimethyl-1,4-phenylene oxide) were utilized in this manuscript to formulate AEMs (anion exchange membranes) for DD (diffusion dialysis) using the phase-inversion technique. FTIR (Fourier transfer infrared) analysis, proton NMR spectroscopy, morphology, IEC (ion exchange capacity), LER (linear expansion ratio), CR (fixed group concentration), WR (water uptake/adsorption), water contact angle, chemical, and thermal stability, were all used to evaluate the prepared membranes. The effect of TMA content within the membrane matrix on acid recovery was also briefly discussed. It was reported that porous AEMs have a WR of 149.6% to 233.8%, IEC (ion exchange capacity) of 0.71 to 1.43 mmol/g, CR (fixed group concentration) that ranged from 0.0046 mol/L to 0.0056 mol/L, LER of 3.88% to 9.23%, and a water contact angle of 33.10° to 78.58°. The UH (acid dialysis coefficients) for designed porous membranes were found to be 0.0043 to 0.012 m/h, with separation factors (S) ranging from 13.14 to 32.87 at the temperature of 25 °C. These observations are comparable to those found in the DF-120B commercial membrane with UH of 0.004 m/h and S of 24.3 m/h at the same temperature (25 °C). This porous membranes proposed in this paper are excellent choices for acid recovery through the diffusion dialysis process.

Asymmetric Pendrin Homodimer Reveals its Molecular Mechanism as Anion Exchanger

Pendrin SLC26A4 is an anion exchanger expressed in apical membranes of selected epithelia. Pendrin ablation causes Pendred syndrome, a genetic disorder disease associated with sensorineural hearing loss, hypothyroid goiter, and reduced blood pressure. However, its molecular structure has remained unknown limiting our understanding. Here, we determined the structures of mouse pendrin with symmetric and characteristically asymmetric homodimer conformations by cryo-electron microscopy. The asymmetric homodimer consists of an inward-facing protomer and an intermediate-state protomer, representing the coincident uptake and secretion process, and exhibits the unique state of pendrin as an electroneutral exchanger. This previously unrevealed conformation, together with other conformations we captured, provides an inverted alternate-access mechanism for anion exchange. Furthermore, our structural and functional data disclosed the properties of anion exchange cleft and interpreted the important pathogenetic mutations. These investigations shed light on the pendrin exchange mechanism and extend our structure-guided understanding of pathogenetic mutations.