Biodegradable Pea Protein Fibril Hydrogel-Based Quasi-Solid-State Zn-Ion Battery

Zinc-ion batteries show great potential as the next-generation power source due to their nontoxic, low-cost, and safe properties. However, issues with zinc anodes, such as dendrite growth and parasitic hydrogen evolution reactions (HERs), must be addressed to commercialize them. Solutions, such as quasi-solid-state electrolytes made from synthetic polymer hydrogels, have been proposed to improve battery flexibility and energy density. However, most polymers used are nonbiodegradable, posing a challenge to sustainability. In this study, hydrogels made from biodegradable poly(vinyl alcohol) and protein nanofibrils from pea protein, a renewable plant-based source, are used as an electrolyte in aqueous zinc-ion batteries. Results show that the flexible and biodegradable hydrogel can enhance the zinc anode stability and effectively restrict HER. This phenomenon is because of the hydrogen-bond network between nanofibril functional groups and water molecules. In addition, the interaction between functional groups on nanofibrils and Zn2+ constructs ion channels for the even migration of Zn2+, avoiding dendrite growth. The Zn||Zn symmetric cell using the hydrogel electrolyte exhibits a long lifespan of over 3000 h and improved capacity retention in the Zn||AC-I2 hybrid ion batteries by suppressing cathode material dissolution. This study suggests the potential of biodegradable hydrogels as a sustainable and effective solution for biodegradable soft powering sources

Детство последней вьюгой улетело

Детство последней вьюгой улетело, / И весной, как-то майским днем, / Юность на меня мундир одела, / Обхватила талию ремнем

Additional file 3: of Basic leucine zipper transcription factor SlbZIP1 mediates salt and drought stress tolerance in tomato

Table S1. Gene products of annotated genes or with sequence similarity showing at least 2-fold change in transcript abundance (p < 0.05) in leaves of SlbZIP1-RNAi line Ri2 compared with WT plants. (XLSX 76 kb

Additional file 5: of Basic leucine zipper transcription factor SlbZIP1 mediates salt and drought stress tolerance in tomato

Figure S4. Hairpin construct of the SlbZIP1 gene for double-stranded RNAi vector. (DOCX 96 kb

MCAD mRNA in C, R, H, R+H groups of the three geno-type mice.

<p>* significantly different from the control group, p<0.05; ** p<0.01. # significantly different from the same group in WT, p<0.01; ## p<0.01.</p

Additional file 2: of Basic leucine zipper transcription factor SlbZIP1 mediates salt and drought stress tolerance in tomato

Figure S2. Multiple sequence alignment among SlbZIP1, SlbZIP07, SlbZIP10 and SlbZIP39 genes. (DOCX 570 kb

Additional file 6: of Basic leucine zipper transcription factor SlbZIP1 mediates salt and drought stress tolerance in tomato

Table S2. Specific primer sequences used for cloning procedure and qRT-PCR analysis. (DOCX 18 kb

Additional file 7: of Basic leucine zipper transcription factor SlbZIP1 mediates salt and drought stress tolerance in tomato

Table S3. The quantitative information of the RNA-seq data. (DOCX 17 kb

Additional file 1: of Basic leucine zipper transcription factor SlbZIP1 mediates salt and drought stress tolerance in tomato

Figure S1. Relative expression profiles of SlbZIP07, SlbZIP10 and SlbZIP39 in the leaves of WT and SlbZIP1-RNAi lines under normal conditions. (DOCX 77 kb

Expression of the HIV-1 <i>PR</i> gene prevents cellular growth and causes oxidative stress, changes of mitochondrial morphology, and cell death in fission yeast.

<p>(<b>A</b>) Inducible expression of the HIV-1 <i>PR</i> gene in RE294 was detected 24 hrs after gene induction by western blot analysis (<b>a</b>). Lane 1, <i>PR</i>-repressing cells; lane 2, <i>PR</i>-inducing cells. Blot shows a 12-kDa protein band that specifically reacted to an antiserum against HIV-1 PR. Expression of the <i>PR</i> gene induced cellular growth arrest in liquid medium (<b>b</b>) and prevented yeast colony formation on agar plates (<b>c</b>) and in liquid medium (<b>d</b>). <i>PR</i>-off, <i>i</i>.<i>e</i>., no PR protein production. <i>PR</i>-on, <i>i</i>.<i>e</i>., PR protein production. All cells were grown at 30°C, and the cell growth was measured at OD₆₅₀ in the time period shown using a spectrophotometer. Pictures of agar plates were taken 6 days after incubation at 30°C under the indicated conditions. Error bars shown in (<b>b</b>) of the growth assay represent at least three independent experiments. (<b>B</b>) HIV-1 <i>PR</i> expression induced cell death (<b>a</b>), oxidative stress (<b>b</b>), and mitochondrial morphological changes (<b>c</b>) in fission yeast. Twenty-four hours after inducible <i>PR</i> expression, cell viability was measured by the yeast live/dead assay [<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0151286#pone.0151286.ref030" target="_blank">30</a>, <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0151286#pone.0151286.ref033" target="_blank">33</a>] (<b>a</b>). In this assay, viable cells are typically shown in orange-red color (left, <i>PR</i>-off); metabolically deceased cells are shown in green-yellow color (right, <i>PR</i>-on). The production of reactive oxygen species (ROS) was measured by an ROS indicator dye DHE (<b>b</b>). Mitochondrial morphologies (<b>c</b>) were visualized by staining fission yeast cells with a mitochondria-specific fluorescent probe, DASPMI, as previously described [<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0151286#pone.0151286.ref022" target="_blank">22</a>, <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0151286#pone.0151286.ref036" target="_blank">36</a>]. Note that normal mitochondria appear like a thread or necklace of multiple small dots concentrated around the edge a cell, at the growing ends of the cell, or as a tubular network extended along the periphery of the cell (Fig 1B-b, left). In contrast, different sizes of mitochondrial aggregates that are situated almost randomly throughout the <i>PR</i>-expressing cells are shown here, indicating changes in mitochondrial morphology (Fig 1B-b, right).</p