A kinetic template effect in the metal ion-catalysed formation of arylphosphonium salts

Tertiary phosphines react with $\text{o}$-halobenzaldimines and $\text{o}$-bromodiarylazo compounds, under mild conditions in the presence of a metal ion catalyst, with displacement of the halogen to form the related arylphosphonium salts. The corresponding $\text{o}$-haloaryl compounds do not undergo these reactions.     

Aqueous latex/ceramic nanoparticle dispersions: colloidal stability and coating properties

The effect of pH on the colloidal stability of aqueous dispersions containing antimony-doped tin oxide (ATO) or indium tin oxide (ITO) nanoparticles and poly(vinyl acetate-acrylic) copolymer (PVAc-co-acrylic) latex particles was investigated using experimental observations and Derjiaguin, Landau, Verwey and Overbeek (DLVO) theory. The microstructure, electrical properties and optical properties of composite coatings prepared from various dispersions were also studied. Zeta potential measurements revealed that the isoelectric point (IEP) of ATO nanoparticles was below pH 2.0, that of ITO nanoparticles was at pH approximately 6.0 and that of PVAc-co-acrylic latex was at pH approximately 2.0. ATO/PVAc-co-acrylic dispersions prepared at pH 3 were stable, but those prepared at pH 1.5 formed aggregates, which settled quickly with time. DLVO theory predictions are in accord with these results. Stable ITO/PVAc-co-acrylic dispersions are obtained at a pH of 3.0 and 11.0, but dispersions are not stable at a pH of 6.0, the IEP of ITO. At a pH of 3.0, DLVO results predict attraction between ITO particles and latex particles. Dispersion pH affected the microstructures and properties of ATO (or ITO)/PVAc-co-acrylic coatings. Suspensions that formed aggregates produced coatings with lower percolation thresholds and lower transparencies than those produced from stable suspensions.     

The effects of immunity and resistance on the development of AIDS

We incorporate basic genetics into an AIDS model. We illustrate that if a homozygote is immune to the disease or is resistant to the effects of the disease, the corresponding allele goes to fixation. On the other hand, if the heterozygote is immune to the disease or is resistant to the effects of the disease, polymorphism usually occurs.     

Synthesis and characterization of thermoreversible biopolymer microgels based on hydrogen bonded nucleobase pairing

We describe the synthesis and characterization of a thermoreversibly cross-linked biopolymer microgel based on protein, DNA, and peptide nucleic acid (PNA) components. The DNA assembles into a trifunctional three-way junction (TWJ) with single-stranded overhangs. PNA oligomers complementary to these overhangs and bearing terminal biotin groups hybridize to the DNA TWJ and simultaneously bind to the tetrafunctional protein avidin, leading to a cross-linked system. Dynamic light scattering experiments reveal that micron-sized particles are formed. Static light scattering was used to characterize the internal structure of these microgels, which were found to have a fractal dimension of 1.85, indicative of a loose network structure. Heating disrupts the weakest component in the system, namely the PNA-DNA hybrid, resulting in dissolution of the microgel, while cooling restores the hydrogen bonding leading to reassembly of the microgel. Variation of the nucleotide sequence permits tuning of the gelation temperature with fine control.     

Aromatic amine coupling ofaspergillus niger lactase to controlled-pore silica witho-dianisidine

Lactose (β-galactosidase) derived fromAspergillus niger was immobilized on controlledpore silica with an average pore diameter of 425 Å. The coupling of this enzyme to the surface of the silica was accomplished by reacting the surface of the silica with o-dianisidine followed by the functionalization of the residual amine with glutaraldehyde or with nitrite to form the diazonium salt. The PH profiles of the immobilized enzymes were determined and compared. Continuous reactor studies of the glutaraldehyde-functionalized, immobilized enzyme indicated a half-life of 52 days at 50°C with a 5% lactose feed at pH 3.5.