Some Uptake Studies of Metal Ions and the Formation of Cu₂0 Particles in Wool

<p>This research programme is concerned with the uptake studies of Cu2+, Zn2+ and Mn2+ at different conditions, by merino wool fibres and also uptake studies of Cu2+ ions by chemically modified wool fibres. Cu2O particles and Cu complexes are formed within merino wool by an in situ reaction with sodium borohydride and thioglycoloic acid respectively. The d-block elements have the ability to bind chemically to certain functional groups present within the keratin protein of wool. The absorption of the Cu2+, Mn2+ and Zn2+ from solution by wool fibres under different conditions notably, time, temperature and initial concentration have been studied. The optimum temperature and reaction time to give highest absorption of the Cu2+ by the wool fibre was found to be 90 oC and one hour without modifying the nature of the wool, from a solution of Cu2+ concentration of 450 mg L-1. Cu2+ was found to give the greatest absorption by the wool fibres, whereas Zn2+ and Mn2+ were found to be absorbed the least. The absorption of Cu2+ ions increases with increasing temperature. At the higher temperature of 90 oC, the -S-S- bonds in the cystine amino acids break more readily, generating thiol and cysteic acid groups to bind with copper ions. The uptake of Cu2+ by ethylenediaminetetraacetic dianhydride (14 mg g-1 of wool) or thioglycolic acid (42.5 mg g-1 of wool) or sodium borohydride (41.8 mg g-1 of wool) treated merino wool fibres increases with respect to unmodified wool (8 mg g-1 of wool). NaBH4 treated merino wool reduces Cu2+ ions to Cu2O particles which form within the wool fibres by an in situ reaction. TGA treated merino wool provides additional functional groups to bind with copper ions and Cu2O particles also likely to be formed within TGA treated wool composites. The metal ions were absorbed into the fibres under various conditions and the extent of absorption was quantified. The form and binding of the Cu2O particles or Cu2+ ions onto the wool fibres are studied using UV-Visible, FTIR, XRD, SEM, EDS and TEM methods.</p>

Some Uptake Studies of Metal Ions and the Formation of Cu₂0 Particles in Wool

<p>This research programme is concerned with the uptake studies of Cu2+, Zn2+ and Mn2+ at different conditions, by merino wool fibres and also uptake studies of Cu2+ ions by chemically modified wool fibres. Cu2O particles and Cu complexes are formed within merino wool by an in situ reaction with sodium borohydride and thioglycoloic acid respectively. The d-block elements have the ability to bind chemically to certain functional groups present within the keratin protein of wool. The absorption of the Cu2+, Mn2+ and Zn2+ from solution by wool fibres under different conditions notably, time, temperature and initial concentration have been studied. The optimum temperature and reaction time to give highest absorption of the Cu2+ by the wool fibre was found to be 90 oC and one hour without modifying the nature of the wool, from a solution of Cu2+ concentration of 450 mg L-1. Cu2+ was found to give the greatest absorption by the wool fibres, whereas Zn2+ and Mn2+ were found to be absorbed the least. The absorption of Cu2+ ions increases with increasing temperature. At the higher temperature of 90 oC, the -S-S- bonds in the cystine amino acids break more readily, generating thiol and cysteic acid groups to bind with copper ions. The uptake of Cu2+ by ethylenediaminetetraacetic dianhydride (14 mg g-1 of wool) or thioglycolic acid (42.5 mg g-1 of wool) or sodium borohydride (41.8 mg g-1 of wool) treated merino wool fibres increases with respect to unmodified wool (8 mg g-1 of wool). NaBH4 treated merino wool reduces Cu2+ ions to Cu2O particles which form within the wool fibres by an in situ reaction. TGA treated merino wool provides additional functional groups to bind with copper ions and Cu2O particles also likely to be formed within TGA treated wool composites. The metal ions were absorbed into the fibres under various conditions and the extent of absorption was quantified. The form and binding of the Cu2O particles or Cu2+ ions onto the wool fibres are studied using UV-Visible, FTIR, XRD, SEM, EDS and TEM methods.</p>

Vibrational Study on Structure and Bioactivity of Protein Fibers Grafted with Phosphorylated Methacrylates

In the last decades, silk fibroin and wool keratin have been considered functional materials for biomedical applications. In this study, fabrics containing silk fibers from Bombyx mori and Tussah silk fibers from Antheraea pernyi, as well as wool keratin fabrics, were grafted with phosmer CL and phosmer M (commercial names, i.e., methacrylate monomers containing phosphate groups in the molecular side chain) with different weight gains. Both phosmers were recently proposed as flame retarding agents, and their chemical composition suggested a possible application in bone tissue engineering. IR and Raman spectroscopy were used to disclose the possible structural changes induced by grafting and identify the most reactive amino acids towards the phosmers. The same techniques were used to investigate the nucleation of a calcium phosphate phase on the surface of the samples (i.e., bioactivity) after ageing in simulated body fluid (SBF). The phosmers were found to polymerize onto the biopolymers efficiently, and tyrosine and serine underwent phosphorylation (monitored through the strengthening of the Raman band at 1600 cm−1 and the weakening of the Raman band at 1400 cm−1, respectively). In grafted wool keratin, cysteic acid and other oxidation products of disulphide bridges were detected together with sulphated residues. Only slight conformational changes were observed upon grafting, generally towards an enrichment in ordered domains, suggesting that the amorphous regions were more prone to react (and, sometimes, degrade). All samples were shown to be bioactive, with a weight gain of up to 8%. The most bioactive samples contained the highest phosmers amounts, i.e., the highest amounts of phosphate nucleating sites. The sulphate/sulphonate groups present in grafted wool samples appeared to increase bioactivity, as shown by the five-fold increase of the IR phosphate band at 1040 cm−1.

Sheep Wool Humidity under Electron Irradiation Affects Wool Sorptivity towards Co(II) Ions

The effect of humidity on sheep wool during irradiation by an accelerated electron beam was examined. Each of the samples with 10%, 53%, and 97% relative humidity (RH) absorbed a dose of 0, 109, and 257 kGy, respectively. After being freely kept in common laboratory conditions, the samples were subjected to batch Co(II) sorption experiments monitored with VIS spectrometry for different lapses from electron beam exposure. Along with the sorption, FTIR spectral analysis of the wool samples was conducted for cysteic acid and cystine monoxide, and later, the examination was completed, with pH measuring 0.05 molar KCl extract from the wool samples. Besides a relationship to the absorbed dose and lapse, the sorptivity results showed considerable dependence on wool humidity under exposure. When humidity was deficient (10% RH), the sorptivity was lower due to limited transformation of cystine monoxide to cysteic acid. The wool pre-conditioned at 53% RH, which is the humidity close to common environmental conditions, demonstrated the best Co(II) sorptivity in any case. This finding enables the elimination of pre-exposure wool conditioning in practice. Under excessive humidity of 97% RH and enough high dose of 257 kGy, radiolysis of water occurred, deteriorating the sorptivity. Each wool humidity, dose, and lapse showed a particular scenario. The time and humidity variations in the sorptivity for the non-irradiated sample were a little surprising; despite the absence of electron irradiation, relevant results indicated a strong sensitivity to pre-condition humidity and lapse from the start of the monitoring.

Accurate characterization of β-amyloid (Aβ40, Aβ42) standards using species-specific isotope dilution by means of HPLC-ICP-MS/MS

The amyloid β peptide, as one of the main components in senile plaque, represents a defining pathological feature for Alzheimer’s disease, and is therefore commonly used as a biomarker for this disease in clinical analysis. However, the selection of suitable standards is limited here, since only a few are commercially available, and these suffer from varying purity. Hence, the accurate characterization of these standards is of great importance. In this study, we developed a method for the traceable quantification of the peptide content using species-specific isotope dilution and ICP-MS/MS detection. It is based on the separation of the sulfur-containing amino acids methionine and cysteine after oxidation and hydrolysis of the peptide. Using a strong anion exchange column, both amino acids could be separated from each other, as well as from their oxidized forms and sulfate. The sulfur content was determined via ICP-MS/MS using oxygen as reaction gas. Species-specific isotope dilution was enabled by using a 34S-labeled yeast hydrolysate, containing methionine sulfone and cysteic acid with different isotopic composition. The peptide contents of Aβ standards (Aβ40,42), as well as myoglobin and lysozyme with different degrees of purity, were determined. For validation purposes, the standard reference material NIST 2389a, which contains the amino acids in a similar concentration, was subjected to the developed sample preparation and analysis method. In addition to accounting for errors during sample preparation, high levels of accuracy and precision could be obtained using this method, making it fit-for-purpose for the characterization of peptide standards. Graphical abstract

A Novel, Easy Assay Method for Human Cysteine Sulfinic Acid Decarboxylase

Cysteine sulfinic acid decarboxylase catalyzes the last step of taurine biosynthesis in mammals, and belongs to the fold type I superfamily of pyridoxal-5′-phosphate (PLP)-dependent enzymes. Taurine (2-aminoethanesulfonic acid) is the most abundant free amino acid in animal tissues; it is highly present in liver, kidney, muscle, and brain, and plays numerous biological and physiological roles. Despite the importance of taurine in human health, human cysteine sulfinic acid decarboxylase has been poorly characterized at the biochemical level, although its three-dimensional structure has been solved. In the present work, we have recombinantly expressed and purified human cysteine sulfinic acid decarboxylase, and applied a simple spectroscopic direct method based on circular dichroism to measure its enzymatic activity. This method gives a significant advantage in terms of simplicity and reduction of execution time with respect to previously used assays, and will facilitate future studies on the catalytic mechanism of the enzyme. We determined the kinetic constants using L-cysteine sulfinic acid as substrate, and also showed that human cysteine sulfinic acid decarboxylase is capable to catalyze the decarboxylation—besides its natural substrates L-cysteine sulfinic acid and L-cysteic acid—of L-aspartate and L-glutamate, although with much lower efficiency.

Tannin-Mordant Coloration with Matcha (camelia sinensis) and Iron(II)-Lactate on Human Hair Tresses

The aim of this work was to optimize our natural hair dyeing system which we described in our previous work and to compare with other dyeing systems. Therefore, we investigated concentration limits of matcha and mordant and compared this new dyeing method with commercial permanent systems on the market. Completely unpigmented hair tresses were dyed with matcha powder (camelia sinensis) and iron(II)-lactate. To investigate the wash fastness and concentration limits, the differently dyed hair tresses were spectrophotometrically measured. The comparison of the damage potential for which cysteic acid is an indicator was measured by NIR. The concentration of matcha and mordant are responsible for the intensity of the color results. The higher the matcha or the mordant concentration, the darker the color results of the dyed hair tresses. Hair damage of matcha mordant dyeing is comparable with results of commercial permanent hair coloration systems. Moreover, the results of wash fastness of matcha mordant dyed hair tresses is comparable and even better by tendency to permanent colored hair tresses.