Luminescent probes for the bioimaging of small anionic species in vitro and in vivo

The ability to spatiotemporally identify the formation of specific anionic species, or track changes in their concentration inside living systems, is of critical importance in deciphering their exact biological roles and effects. The development of probes (also called bioimaging agents and intracellular sensors) to achieve this goal has become a rapidly growing branch of supramolecular chemistry. In this critical review the challenges specific to the task are identified and for a select range of small anions of environmental and biological relevance (fluoride, chloride, iodide, cyanide, pyrophosphate, bicarbonate, hydrosulphide, peroxynitrite, hypochlorite and hypobromite) a comprehensive overview of the currently available in vitro and in vivo probes is provided.

Hydrolysis of (Me3SiCH2)PhSnCl2. Isomerisation of the dimeric tetraorganodistannoxane [(Me3SiCH2)Ph(Cl)SnOSn(Cl)-Ph(CH2SiMe3)]2

The hydrolysis of (Me₃SiCH₂)PhSnCl₂( 1) was studied under two different reaction conditions (i) by using an excess of aqueous NaOH in toluene at reflux temperature and (ii) by using small amounts of NEt₃ and water in CH₂Cl₂ at room temperature. For (i) the products  (Me₃SiCH₂)Ph₂SnOSnPh₂(CH₂SiMe₃)( 2) and [(Me₃SiCH₂Sn)₁₂O₁₄(OH)₆](OH)₂( 3) were isolated indicating that a phenyl group migration took place. For (ii) the dimeric tetraorganodistannoxane [(Me₃SiCH₂)Ph(Cl)SnOSn(Cl)Ph(CH₂SiMe₃)]₂( 4) was obtained. In solution, 4 exists as an equilibrium mixture of all five possible isomers 4a–4e; in the solid state two of these isomers 4d and 4e co-crystallized in the same crystal modification. The observation of interconvertible isomers of 4 was attributed to the kinetic lability of the ladder-like Sn4O2Cl4 structural motif. Compounds 1 and 4 were investigated by X-ray crystallography.

The use of artificial biofilms to strip nutrients from an industrial smelters waste water under conditions of low temperature and high pH

The Victorian Environment Protection Authority (EPA) has identified Alcoa’s Point Henry aluminium smelter as being a major source of recognized pollutant input due to its disposal of effluent into Corio Bay. Historically, the water quality parameters that have most often exceeded Point Henry’s EPA limits have been pH and suspended solids from the smelter’s discharge points. These waste water discharges also experience high nitrogen and phosphorus concentrations which result in algal blooms that occur at the onset of warm weather. The main hypothesis of this study was that “prevention of algal blooming with the onset of warm weather by removal of nutrients during the cooler months, and continued removal thereafter, is better than curing the problems chemically”. Biofilms have been used to remove nutrients from waste waters, but not under the conditions experienced at Point Henry. The aim of this study, therefore, was to determine if significant biofilm growth would be observed on floating structures suspended in the Point Henry waste water stream during the cooler, winter months of the year. Statistically significant biofilm growth occurred on all suspended structures in all discharge ponds during the winter and early spring of 2000. The use of suspended structures, such as AquaMatTM, as an artificial substrate to attract and support periphyton and bacterial communities (biofilms), which are then able to out-compete phytoplankton communities for available nutrients, is therefore a viable option for the Point Henry smelter. However, further research on the competitive performance of biofilms in the Point Henry ponds during the summer months is required before adequate biofilm management strategies can be developed.

The effect of pH on wool fiber diameter and fabric dimensions

Wool fabrics are often treated under conditions of varying pH in dyeing and finishing processes. It is known that in air the dimensions of wool fabrics change with the amount of fiber swelling at different regain. In this work, it has been shown that a similar relationship between fiber swelling and fabric dimensions existed in water at different pH values. The diameters of Merino and Corriedale wool fibers in water at different pH values were measured with an OFDA 2000 fiber diameter analyzer, fitted with a specially constructed accessory liquid cell. The results showed that the mean diameters of swollen wool fibers in water varied with pH. Minimum swelling was obtained in the range pH 5-7. It was found that the dimensions of wool fabric in water were dependent on the pH. The changes in fiber diameter in water could be attributed to changes in ionic interactions between charged acid and basic groups in wool protein with variations in pH.

Investigating the effect of solution pH on speciation of La(4OH-cin)3 with correlation to electrochemical behaviour and corrosion efficiency

The nature of the species in solution plays a major role on the effectiveness of the corrosion inhibitor on a steel substrate. The speciation of lanthanum 4-hydroxy cinnamate (La(4OHCin) ₃) in solution has been evaluated using experimental techniques composed of potentiodynamic polarisation, immersion tests, nuclear magnetic spectroscopy and mass spectroscopy. It is evident that the species in solution are dependent on pH and this impacts the corrosion inhibition mechanism and the efficiency. It was found that at a neutral pH of 5.5 the La(4OH-Cin)₃ behaves as a strong anodic inhibitor. Whereas, when the pH shifts to low (pH2.5) and/or high (pH8) the corrosion mechanism changes.

Unification of the copper(I) binding affinities of the metallo-chaperones Atx1, Atox1, and related proteins : Detection probes and affinity standards

Literature estimates of metal-protein affinities are widely scattered for many systems, as highlighted by the class of metallo-chaperone proteins, which includes human Atox1. The discrepancies may be attributed to unreliable detection probes and/or inconsistent affinity standards. In this study, application of the four CuI ligand probes bicinchoninate, bathocuproine disulfonate, dithiothreitol (Dtt), and glutathione (GSH) is reviewed, and their CuI affinities are re-estimated and unified. Excess bicinchoninate or bathocuproine disulfonate reacts with CuI to yield distinct 1:2 chromatophoric complexes [CuIL2] 3- with formation constants β2 = 1017.2 and 1019.8 M-2, respectively. These constants do not depend on proton concentration for pH ≥7.0. Consequently, they are a pair of complementary and stable probes capable of detecting free Cu+ concentrations from 10-12 to 10-19 M. Dtt binds CuI with KD∼10-15 M at pH 7, but it is air-sensitive, and its CuI affinity varies with pH. The CuI binding properties of Atox1 and related proteins (including the fifth and sixth domains at the N terminus of the Wilson protein ATP7B) were assessed with these probes. The results demonstrate the following: (i) their use permits the stoichiometry of high affinity CuI binding and the individual quantitative affinities (KD values) to be determined reliably via noncompetitive and competitive reactions, respectively; (ii) the scattered literature values are unified by using reliable probes on a unified scale; and (iii) Atox1-type proteins bind CuI with sub-femtomolar affinities, consistent with tight control of labile Cu+ concentrations in living cells.

Effects of pH on the stress-strain properties of wool fabric

In wool dyeing and finishing processes, fabric is often treated under conditions of different pHs and is subjected to a variety of physical and chemical environments. This work investigates fabric tensile properties at three different fabric pHs. Wool fabric extensibility under a 5 N/cm load was observed to be greatest at the wool isoelectric point of pH 4.8 and lower at both pH 2.1 and pH 7.2. The impact of pH on fabric extensibility was found to be similar to the variation in fabric hygral expansion previously observed. Fabric stress–strain curves at different pHs showed that for a given fabric extension level, the work required to stretch a fabric was less at pH 2.1 than at pH 4.8. These results suggest that the strength of wool fabric is at maximum when the pH of the fibres is close to the wool isoelectric point and that for consistency, the pH of fabric should be adjusted before standard strength tests are carried out.

Tuning the mechanical and morphological properties of self-assembled peptide hydrogels via control over the gelation mechanism through regulation of ionic strength and the rate of pH change

Hydrogels formed by the self-assembly of peptides are promising biomaterials. The bioactive and biocompatible molecule Fmoc-FRGDF has been shown to be an efficient hydrogelator via a π-β self-assembly mechanism. Herein, we show that the mechanical properties and morphology of Fmoc-FRGDF hydrogels can be effectively and easily manipulated by tuning both the final ionic strength and the rate of pH change. The increase of ionic strength, and consequent increase in rate of gelation and stiffness, does not interfere with the underlying π-β assembly of this Fmoc-protected peptide. However, by tuning the changing rate of the system's pH through the use of glucono-δ-lactone to form a hydrogel, as opposed to the previously reported HCl methodology, the morphology (nano- and microscale) of the scaffold can be manipulated.