Nanofiltration Process for Enhanced Treatment of RO Brine Discharge

Brine discharge of reverse osmosis (RO) desalination plants represents a challenge for both inland and coastal desalination plants. Zero-liquid discharge (ZLD) can be accomplished by using additional stages of RO, which can recycle that brine water, but the key challenge is the high concentration of divalent salts. These divalent salts (especially calcium and magnesium salts) forms a scaling layer on the RO membrane surfaces and hence shorten the life-time of the membranes. In this study, the nanofiltration (NF) procedure was used to remove divalent ions from the brine discharge to minimize the load on additional stages of RO membranes. One of the most critical considerations influencing the selection of an effective NF is the water type, which is expected here by calculation of some hydrochemical parameters (major ions, hypothetical soluble salts (electrolyte), and saturation indices). NF experiments were undertaken on a lab-scale using a low-pressure hand-made system of 4–7 bar. Synthetic single salts solutions and two real brine water discharge (brackish (BWRO) and seawater (SWRO) desalination plants) were used as a feed solution for NF system. The chemical characteristics of the RO-feed, RO-brine, NF-permeate, and NF-reject in were investigated. Electrolyte concentrations and saturation indices were determined based on the concentration of the major ions and the NETPATH software package, respectively. Calculations reveal that the brine concentrate samples contained mostly MgSO4 and MgCl2 soluble salts. The results show that 79–89% of the total dissolved salts (TDS) and 96–98% of the total hardness (TH) were retained using the NF process. The salt rejection of the NF membrane follows the order of CaSO4, Na2SO4, MgSO4, MgCl2, and NaCl with a percent of 97.4, 97.3, 95.2, 93.4, and 79%, respectively.

Structural Analysis of the cl-Par-4 Tumor Suppressor as a Function of Ionic Environment

Prostate apoptosis response-4 (Par-4) is a proapoptotic tumor suppressor protein that has been linked to a large number of cancers. This 38 kilodalton (kDa) protein has been shown to be predominantly intrinsically disordered in vitro. In vivo, Par-4 is cleaved by caspase-3 at Asp-131 to generate the 25 kDa functionally active cleaved Par-4 protein (cl-Par-4) that inhibits NF-κB-mediated cell survival pathways and causes selective apoptosis in tumor cells. Here, we have employed circular dichroism (CD) spectroscopy and dynamic light scattering (DLS) to assess the effects of various monovalent and divalent salts upon the conformation of cl-Par-4 in vitro. We have previously shown that high levels of sodium can induce the cl-Par-4 fragment to form highly compact, highly helical tetramers in vitro. Spectral characteristics suggest that most or at least much of the helical content in these tetramers are non-coiled coils. Here, we have shown that potassium produces a similar effect as was previously reported for sodium and that magnesium salts also produce a similar conformation effect, but at an approximately five times lower ionic concentration. We have also shown that anion identity has far less influence than does cation identity. The degree of helicity induced by each of these salts suggests that the “Selective for Apoptosis in Cancer cells” (SAC) domain—the region of Par-4 that is most indispensable for its apoptotic function—is likely to be helical in cl-Par-4 under the studied high salt conditions. Furthermore, we have shown that under medium-strength ionic conditions, a combination of high molecular weight aggregates and smaller particles form and that the smaller particles are also highly helical, resembling at least in secondary structure, the tetramers found at high salt.

Organization and Regulation of Chromatin by Liquid-Liquid Phase Separation

Genomic DNA is highly compacted in the nucleus of eukaryotic cells as a nucleoprotein assembly called chromatin1. The basic unit of chromatin is the nucleosome, where ∼146 base pair increments of the genome are wrapped and compacted around the core histone proteins2,3. Further genomic organization and compaction occur through higher order assembly of nucleosomes4. This organization regulates many nuclear processes, and is controlled in part by histone post-transtranslational modifications and chromatin-binding proteins. Mechanisms that regulate the assembly and compaction of the genome remain unclear5,6. Here we show that in the presence of physiologic concentrations of mono- and divalent salts, histone tail-driven interactions drive liquid-liquid phase separation (LLPS) of nucleosome arrays, resulting in substantial condensation. Phase separation of nucleosomal arrays is inhibited by histone acetylation, whereas histone H1 promotes phase separation, further compaction, and decreased dynamics within droplets, mirroring the relationship between these modulators and the accessibility of the genome in cells7-10. These results indicate that under physiologically relevant conditions, LLPS is an intrinsic behavior of the chromatin polymer, and suggest a model in which the condensed phase reflects a genomic “ground state” that can produce chromatin organization and compaction in vivo. The dynamic nature of this state could enable known modulators of chromatin structure, such as post-translational modifications and chromatin binding proteins, to act upon it and consequently control nuclear processes such as transcription and DNA repair. Our data suggest an important role for LLPS of chromatin in the organization of the eukaryotic genome.

Influence of ions to modulate hydrazone and oxime reaction kinetics to obtain dynamically cross-linked hyaluronic acid hydrogels

Simple monovalent and divalent salts are presented as a novel catalyst for performing hydrazone and oxime coupling chemistry at physiological pH with excellent yields.

Effects of mono- and divalent cations on the structure and thermodynamic properties of polyelectrolyte gels

Measurements are reported on the effect of monovalent and divalent salts on the swelling behavior and supramolecular structure of sodium polyacrylate gels (NaPA) made by osmotic swelling pressure and small angle neutron scattering measurements.