Carbon nanotube–polyaniline composites

The last decade has seen a growing interest in hybrid electrically conducting nanocomposites. This article aims to provide a detailed overview of the present status of research in carbon nanotube–polyaniline (CNT/PANI) composites, from processing to structural and property evaluations. CNT/PANI are synthesized by electrochemical and chemical processing. When chemical methods are used, the main challenge is to obtain processable CNT/PANI in the emeraldine salt (ES) form composites. Stable dispersions of ES–CNT in organic media are prepared using the post doping method, inverse emulsion polymerization, or ex situ polymerizations. On the contrary, stable water dispersions of CNT/ES are prepared using hydrophilization of a preformed CNT/ES composite, direct synthesis of micelle–CNT hybrid templates, interfacial polymerization, covalent functionalization of CNT with a water soluble polymer, or using electrostatic interactions between two oppositely charged ES and CNT aqueous colloids. Moreover, the strategies for the synthesis of ternary CNT/PANI composites incorporating noble metal nanoparticles, metal oxide, or graphene sheets are also presented and analyzed in depth. Finally, we give a review of potential applications, including chemical sensors, capacitors, fuel cells and electronic devices.     

The Enzymatic and Non-Enzymatic Antioxidant System Response of the Seagrass Cymodocea nodosa to Bisphenol-A Toxicity

The effects of environmentally relevant bisphenol A (BPA) concentrations (0.3, 1 and 3 μg L⁻¹) were tested at 2, 4, 6 and 8 days, on intermediate leaves, of the seagrass Cymodocea nodosa. Hydrogen peroxide (H₂O₂) production, lipid peroxidation, protein, phenolic content and antioxidant enzyme activities were investigated. Increased H₂O₂ formation was detected even at the lowest BPA treatments from the beginning of the experiment and both the enzymatic and non-enzymatic antioxidant defense mechanisms were activated upon application of BPA. Elevated H₂O₂ levels that were detected as a response to increasing BPA concentrations and incubation time, led to the decrease of protein content on the 4th day even at the two lower BPA concentrations, and to the increase of the lipid peroxidation at the highest concentration. However, on the 6th day of BPA exposure, protein content did not differ from the control, indicating the ability of both the enzymatic and non-enzymatic mechanisms (such as superoxide dismutase (SOD) and phenolics) to counteract the BPA-derived oxidative stress. The early response of the protein content determined that the Low Effect Concentration (LOEC) of BPA is 0.3 μg L⁻¹ and that the protein content meets the requirements to be considered as a possible early warning “biomarker” for C. nodosa against BPA toxicity.     

Chloroplast Thylakoidal Ascorbate Peroxidase,PtotAPX, Has Enhanced Resistance to Oxidative Stress in Populus tomentosa

Chloroplasts are the most major producers of reactive oxygen species (ROS) during photosynthesis. However, the function of thylakoid ascorbate peroxidase (tAPX) in response to oxidative stress in wood trees is largely unknown. Our results showed that PtotAPX of Populus tomentosa could effectively utilize ascorbic acid (AsA) to hydrolyze hydrogen peroxide (H₂O₂) in vitro. The overexpression or antisense of PtotAPX (OX-PtotAPX or anti-PtotAPX, respectively) in Populus tomentosa plants did not significantly affect plant morphology during plant growth. When treated with methyl viologen (MV), the OX-PtotAPX plants exhibited less morphological damage under stress conditions compared to WT plants. OX-PtotAPX plants maintained lower H₂O₂ levels and malondialdehyde (MDA) contents, but more reduced AsA levels, a higher photosynthetic rate (Pn), and the maximal photochemical efficiency of PSII (Fv/Fm), whereas anti-PtotAPX plants showed the opposite phenotype. Furthermore, the activity of APX was slightly higher in OX-PtotAPX under normal growth conditions, and this activity significantly decreased after stress treatment, which was the lowest in anti-P. Based on these results, we propose that PtotAPX is important for protecting the photosynthetic machinery under severe oxidative stress conditions in P. tomentosa, and is a potential genetic resource for regulating the stress tolerance of woody plants.     

Repair of Protein Radicals by Antioxidants

In vivo, proteins are the main targets for radicals and other reactive species. Their reactions result in formation of amino acid radicals on the protein surface that often yield tryptophan and tyrosyl radicals or, in the presence of O₂, protein peroxyl radicals and hydroperoxides. All these species may propagate damage to biomolecules. Low molecular weight antioxidants, such as ascorbate, urate, and glutathione, are part of the defense system and function by repairing damaged proteins. We briefly review the existing knowledge about protein and amino acid radicals and their repair by antioxidants, including results of our investigations. The main question addressed is whether the antioxidants ascorbate, urate, and glutathione are able to repair amino acid radicals in model compounds and in proteins in vitro by pulse radiolysis. We show that ascorbate and urate repair tryptophan and tyrosyl radicals efficiently and inhibit proton-coupled electron transfer from tyrosine residues to tryptophan radicals in a number of proteins. In contrast, repair by glutathione is much slower. Ascorbate also rapidly reduces the peroxyl radicals of the N-acetylamide derivatives of glycine, alanine, and proline, whereas glutathione reduces peroxyl radicals in lysozyme. In vivo urate, ascorbate, and glutathione may prevent biological damage or, at least, reduce its rate, because they: (a) repair tryptophan and tyrosyl radicals in proteins and (b) reduce protein peroxyl radicals to the corresponding protein hydroperoxides. Most likely, in vivo, ascorbate and glutathione do not inhibit the reaction of C-centered amino acid radicals with O₂. Glutathione is less efficient that urate and ascorbate in repairing protein radicals; furthermore, the resulting glutathiyl radical is harmful. Ascorbate may be the more important repair agent in cells and tissues characterized by high ascorbate concentrations, such as the lens and brain; urate may be mainly responsible for repair in tissue compartments with higher urate concentrations, such as in plasma and saliva.     

Ascorbate Peroxidase and Catalase Activities and Their Genetic Regulation in Plants Subjected to Drought and Salinity Stresses

Hydrogen peroxide (H₂O₂), an important relatively stable non-radical reactive oxygen species (ROS) is produced by normal aerobic metabolism in plants. At low concentrations, H₂O₂ acts as a signal molecule involved in the regulation of specific biological/physiological processes (photosynthetic functions, cell cycle, growth and development, plant responses to biotic and abiotic stresses). Oxidative stress and eventual cell death in plants can be caused by excess H₂O₂ accumulation. Since stress factors provoke enhanced production of H₂O₂ in plants, severe damage to biomolecules can be possible due to elevated and non-metabolized cellular H₂O₂. Plants are endowed with H₂O₂-metabolizing enzymes such as catalases (CAT), ascorbate peroxidases (APX), some peroxiredoxins, glutathione/thioredoxin peroxidases, and glutathione sulfo-transferases. However, the most notably distinguished enzymes are CAT and APX since the former mainly occurs in peroxisomes and does not require a reductant for catalyzing a dismutation reaction. In particular, APX has a higher affinity for H₂O₂ and reduces it to H₂O in chloroplasts, cytosol, mitochondria and peroxisomes, as well as in the apoplastic space, utilizing ascorbate as specific electron donor. Based on recent reports, this review highlights the role of H₂O₂ in plants experiencing water deficit and salinity and synthesizes major outcomes of studies on CAT and APX activity and genetic regulation in drought- and salt-stressed plants.     

H2O2对家蝇蛹内部几种酶活性的影响

目的研究外源H2O2对家蝇蛹内与抗性相关的几种酶活性的影响。方法通过H2O2诱导,测定家蝇蛹内过氧化氢酶(CAT)、过氧化物酶(POD)、抗坏血酸过氧化物酶(AsA-POD)以及多酚氧化酶(PPO)的活性变化。结果H2O2处理后蛹内CAT和AsA-POD的活性变化规律与处理前差别不大;POD活性在H2O2处理后12h内出现活性高峰,约为对照组的2.5倍,此后稍高于对照组,最后基本与对照组持平;PPO活性在处理后12h内与对照组相当,此后活性骤然升高,处理后24h达到对照组的2.13倍,然后变化速度减慢,但一直维持在对照组的1.3倍左右,48h后活性开始下降。结论H2O2对CAT和AsA-POD的活性影响较小,对POD和PPO的活性有一定的影响。     

Assay of ascorbic phosphates and in-vitro availability assay of ascorbic mono-and polyphosphates

A method was devised to assay ascorbic phosphate esters in biological materials by potassium bromoxide hydrolysis followed by determination of the liberated ascorbic acid. For the differential measurement of ascorbic acid and ascorbic phosphate, a spectrophotometric method was employed to screen out the interfering substances based on studies of absorbance curves of 2,4-dinitrophenyl hydrazine derivatives. A variety of vertebrate tissues were examined for phosphatase activity on ascorbic phosphate esters. The results suggest that pigeon kidney, rat liver and several tissues of fishes readily hydrolyse ascorbic monophosphate but not ascorbic polyphosphate. Hydrolysis of ascorbic monophosphate is completed by both phosphatases of intestine, kidney and liver acting at neutral pH and phosphatase of stomach acting at acid pH. Thus, ascorbic monophosphate has the potential to be a source of available vitamin C in vivo, and this explains its antiscorbutic activity in scurvy-prone animals.     

H2O2对家蝇蛹内部几种酶活性的影响

目的研究外源H2O2对家蝇蛹内与抗性相关的几种酶活性的影响。方法通过H2O2诱导,测定家蝇蛹内过氧化氢酶（CAT）、过氧化物酶（POD）、抗坏血酸过氧化物酶（AsA-POD）以及多酚氧化酶（PPO）的活性变化。结果H2O2处理后蛹内CAT和AsA-POD的活性变化规律与处理前差别不大;POD活性在H2O2处理后12h内出现活性高峰,约为对照组的2.5倍,此后稍高于对照组,最后基本与对照组持平;PPO活性在处理后12h内与对照组相当,此后活性骤然升高,处理后24h达到对照组的2.13倍,然后变化速度减慢,但一直维持在对照组的1.3倍左右,48h后活性开始下降。结论H2O2对CAT和AsA-POD的活性影响较小,对POD和PPO的活性有一定的影响。