The impact of anionic polyacrylamide (APAM) on ultrafiltration efficiency in flocculation-ultrafiltration process.

With the purpose of improving the ultrafiltration (UF) efficiency, anionic polyacrylamide (APAM) has been used as a coagulant aid in the flocculation-UF process. In this study, the impact of APAM on UF efficiency has been investigated with regard to membrane fouling, membrane cleaning and effluent quality. The results indicated that the optimal dosage of APAM had positive impacts on membrane fouling control, membrane cleaning and effluent quality. According to the flux decline curve, scanning electron microscopy and contact angle characterization, the optimal dosage of APAM was determined to be 0.1 mg/L coupled with 2 mg/L (as Al3+) poly-aluminium chloride. Under this optimal condition, membrane fouling can be mitigated because of the formation of a porous and hydrophilic fouling layer. APAM in the fouling layer can improve the chemical cleaning efficiency of 0.5% NaOH due to the disintegration of the fouling layer when APAM is dissolved under strong alkaline conditions. Furthermore, with the addition of APAM in the flocculation-UF process, more active adsorption sites can be formed in the flocs as well as the membrane fouling layer, thus more antipyrine molecules in the raw water can be adsorbed and removed in the flocculation-UF process.

Vaccine-induced HIV-1 envelope gp120 constant region 1-specific antibodies expose a CD4-inducible epitope and block the interaction of HIV-1 gp140 with galactosylceramide.

UNLABELLED: Mucosal epithelial cell surface galactosylceramide (Galcer) has been postulated to be a receptor for HIV-1 envelope (Env) interactions with mucosal epithelial cells. Disruption of the HIV-1 Env interaction with such alternate receptors could be one strategy to prevent HIV-1 entry through the mucosal barrier. To study antibody modulation of HIV-1 Env-Galcer interactions, we used Galcer-containing liposomes to assess whether natural- and vaccine-induced monoclonal antibodies can block HIV-1 Env binding to Galcer. HIV-1 Env gp140 proteins bound to Galcer liposomes with Kds (dissociation constants) in the nanomolar range. Several HIV-1 ALVAC/AIDSVAX vaccinee-derived monoclonal antibodies (MAbs) specific for the gp120 first constant (C1) region blocked Galcer binding of a transmitted/founder HIV-1 Env gp140. Among the C1-specific MAbs that showed Galcer blocking, the antibody-dependent cellular cytotoxicity-mediating CH38 IgG and its natural IgA isotype were the most potent blocking antibodies. C1-specific IgG monoclonal antibodies that blocked Env binding to Galcer induced upregulation of the gp120 CD4-inducible (CD4i) epitope bound by MAb 17B, demonstrating that a conformational change in gp120 may be required for Galcer blocking. However, the MAb 17B itself did not block Env-Galcer binding, suggesting that the C1 antibody-induced gp120 conformational changes resulted in alteration in a Galcer binding site distant from the CD4i 17B MAb binding site. IMPORTANCE: Galactosyl ceramide, a glycosphingolipid, has been postulated to be a receptor for the HIV-1 envelope glycoprotein (Env) interaction with mucosal epithelial cells. Here, we have mimicked this interaction by using an artificial membrane containing synthetic Galcer and recombinant HIV-1 Env proteins to identify antibodies that would block the HIV-1 Env-Galcer interaction. Our study revealed that a class of vaccine-induced human antibodies potently blocks HIV-1 Env-Galcer binding by perturbing the HIV-1 Env conformation.

Synergistic interfacial polymerization between hydramine/diamine and trimesoyl chloride: A novel reaction for NF membrane preparation.

Polyester-amide (PEA) thin film composite (TFC) NF membranes have rapidly evolved towards a competitive performance, benefiting from their remarkable antifouling capability and superior chlorine resistance. In this report, a new concept of synergistic interfacial polymerization is explored, which promptly triggers the reaction between hydramines and trimesoyl chloride (TMC) in the presence of a trace amount of diamines. This rapid-start mode enables the formation of defect-free PEA films without the requirement of catalysis. A comprehensive characterization of physicochemical properties using high-resolution mass spectrometer (HRMS) reveals that the recombination and formation of a "hydramine-diamine" coupling unit plays a decisive role in activating the synergistic interfacial polymerization reaction with TMC molecules. Taking the pair of serinol and piperazine (PIP) as an example, the PEA-NF membrane fabricated with 0.1 w/v% serinol mixed with 0.04 w/v% PIP as water-soluble monomer and 0.1 w/v% TMC as oil phase monomer was found to have a pure water permeability (PWP) of 18.5 L·m-2·h-1·bar-1 and a MgSO4 rejection of 95.5 %, which surpasses almost all the reported PEA NF membranes. Findings of the current research provide more possibilities for the low-cost and rapid synthesis of high-performance PEA membranes aiming for water purification.

Role of HIV membrane in neutralization by two broadly neutralizing antibodies.

Induction of effective antibody responses against HIV-1 infection remains an elusive goal for vaccine development. Progress may require in-depth understanding of the molecular mechanisms of neutralization by monoclonal antibodies. We have analyzed the molecular actions of two rare, broadly neutralizing, human monoclonal antibodies, 4E10 and 2F5, which target the transiently exposed epitopes in the membrane proximal external region (MPER) of HIV-1 gp41 envelope during viral entry. Both have long CDR H3 loops with a hydrophobic surface facing away from the peptide epitope. We find that the hydrophobic residues of 4E10 mediate a reversible attachment to the viral membrane and that they are essential for neutralization, but not for interaction with gp41. We propose that these antibodies associate with the viral membrane in a required first step and are thereby poised to capture the transient gp41 fusion intermediate. These results bear directly on strategies for rational design of HIV-1 envelope immunogens.

Polyamidoamine dendrimer grafted forward osmosis membrane with superior ammonia selectivity and robust antifouling capacity for domestic wastewater concentration.

Developing a forward osmosis (FO) membrane with superior ammonia selectivity and robust antifouling performance is important for treating domestic wastewater (DW) but challenging due to the similar polarities and hydraulic radii of NH4+ and water molecules. Herein, we investigated the feasibility of using polyamidoamine (PAMAM) dendrimer to simultaneously enhance the ammonia rejection rate and antifouling capacity of the thin-film composite (TFC) FO membrane. PAMAM dendrimer with abundant, easily-protonated, terminal amine groups was grafted on TFC-FO membrane surface via covalent bonds, which inspired the TFC-FO membrane surface with appreciable Zeta potential (isoelectric point: pH = 5.5) and outstanding hydrophilicity (water contact angle: 39.83 ±â€¯0.57°). Benefiting from the electrostatic repulsion between the protonated amine layer and NH4+-N as well as the concentration-induced diffusion resistance, the introduction of PAMAM dendrimer endowed the grafted membrane with a superior NH4+-N rejection rate of 98.23% and a significantly reduced the reverse solute flux when using NH4Cl solutions as feed solution. Meanwhile, the perfect balance between the electrostatic repulsion to positively-charged micromoleculer ions (metal ions and NH4+-N) and the electrostatic attraction to negatively-charged macromolecular organic foulants together with the hydrophilic nature of amine groups facilitated the enhancement of the grafted membranes in antifouling capacity and hence the NH4+-N selectivity (rejection rate of 91.81%) during the concentration of raw DW. The overall approach of this work opens up a frontier for preparation of ammonia-selective and antifouling TFC-FO membrane.

Induction of antibodies in rhesus macaques that recognize a fusion-intermediate conformation of HIV-1 gp41.

A component to the problem of inducing broad neutralizing HIV-1 gp41 membrane proximal external region (MPER) antibodies is the need to focus the antibody response to the transiently exposed MPER pre-hairpin intermediate neutralization epitope. Here we describe a HIV-1 envelope (Env) gp140 oligomer prime followed by MPER peptide-liposomes boost strategy for eliciting serum antibody responses in rhesus macaques that bind to a gp41 fusion intermediate protein. This Env-liposome immunization strategy induced antibodies to the 2F5 neutralizing epitope 664DKW residues, and these antibodies preferentially bound to a gp41 fusion intermediate construct as well as to MPER scaffolds stabilized in the 2F5-bound conformation. However, no serum lipid binding activity was observed nor was serum neutralizing activity for HIV-1 pseudoviruses present. Nonetheless, the Env-liposome prime-boost immunization strategy induced antibodies that recognized a gp41 fusion intermediate protein and was successful in focusing the antibody response to the desired epitope.