Novel Quasi‐Liquid K‐Na Alloy as a Promising Dendrite‐Free Anode for Rechargeable Potassium Metal Batteries

Rechargeable potassium metal batteries are promising energy storage devices with potentially high energy density and markedly low cost. However, eliminating dendrite growth and achieving a stable electrode/electrolyte interface are the key challenges to tackle. Herein, a novel "quasi-liquid" potassium-sodium alloy (KNA) anode comprising only 3.5 wt% sodium (KNA-3.5) is reported, which exhibits outstanding electrochemical performance able to be reversibly cycled at 4 mA cm-2 for 2000 h. Moreover, it is demonstrated that adding a small amount of sodium hexafluorophosphate (NaPF6 ) into the potassium bis(fluorosulfonyl)imide electrolyte allows for the formation of the "quasi-liquid" KNA on electrode surface. Comprehensive experimental studies reveal the formation of an unusual metastable KNa2 phase during plating, which is believed to facilitate simultaneous nucleation and suppress the growth of dendrites, thereby improving the electrode's cycle lifetime. The "quasi-liquid" KNA-3.5 anode demonstrates markedly enhanced electrochemical performance in a full cell when pairing with Prussian blue analogs or sodium rhodizonate dibasic as the cathode material, compared to the pristine potassium anode. Importantly, unlike the liquid KNA reported before, the "quasi-liquid" KNA-3.5 exhibits good processability and can be readily shaped into sheet electrodes, showing substantial promise as a dendrite-free anode in rechargeable potassium metal batteries.Z.T. acknowledges the financial support of Maria Curie COFUND fellowship (Grant No. 713640). Z.L. thanks the financial support of China Scholarship Council (Grant No. 201 806 400 066). This project was partly funded by the “Baterias 2030” project through the Mobilizadore Programme by the National Innovation Agency of Portugal (Grant No. POCI-01-0247- FEDER-046109). G.Y. acknowledges the financial support from the Welch Foundation Award F-1861. The authors thank Dr. Artur Martins for his assistance in mechanical property measurement.info:eu-repo/semantics/publishedVersio

Chemical Elucidation of Structurally Diverse Willow Lignins

A new fast-growing wood raw material, willow (Salix matsudana cv. Zhuliu), was subjected to pulping to identify the structure of its lignin. Thus, the black liquor lignin (AL) and enzymatic mild acidolysis lignin (EMAL) were prepared, and their molecular structure and molecular weight of the isolated lignin polymers were comprehensively investigated by Fourier transform infrared spectroscopy (FT-IR), two-dimensional nuclear magnetic resonance (2D-NMR HSQC), 13C nuclear magnetic resonance (13C-NMR), and gel permeation chromatography (GPC). The NMR results showed that syringyl (S) unit was the predominant structural monomeric unit in willow lignin, as opposed to guaiacyl (G) and p-hydroxyphenyl (H) units. The S/G ratio for the EMAL was found to be 2.02, whereas that for the AL was 0.94. The lignin in the black liquor (AL) fraction was modified during pulping, as shown by its reduced molecular weight. The two isolated lignin polymers, EMAL and AL showed low weight-average molecular weight: 4127 g/mol and 3522.5 g/mol, and in addition they exhibited low polydispersity index (Mw/Mn < 2.0)

Crystallization of Galectin-8 Linker Reveals Intricate Relationship between the N-terminal Tail and the Linker

Galectin-8 (Gal-8) plays a significant role in normal immunological function as well as in cancer. This lectin contains two carbohydrate recognition domains (CRD) connected by a peptide linker. The N-terminal CRD determines ligand binding specificity, whereas the linker has been proposed to regulate overall Gal-8 function, including multimerization and biological activity. Here, we crystallized the Gal-8 N-terminal CRD with the peptide linker using a crystallization condition that contains Ni2+. The Ni2+ ion was found to be complexed between two CRDs via crystal packing contacts. The coordination between Ni2+ and Asp25 plays an indirect role in determining the structure of β-strand F0 and in influencing the linker conformation which could not be defined due to its dynamic nature. The linker was also shortened in situ and crystallized under a different condition, leading to a higher resolution structure refined to 1.08 Å. This crystal structure allowed definition of a short portion of the linker interacting with the Gal-8 N-terminal tail via ionic interactions and hydrogen bonds. Observation of two Gal-8 N-terminal CRD structures implies that the N-terminal tail and the linker may influence each other’s conformation. In addition, under specific crystallization conditions, glycerol could replace lactose and was observed at the carbohydrate binding site. However, glycerol did not show inhibition activity in hemagglutination assay

Participation of the Syntaxin 5/Ykt6/GS28/GS15 SNARE Complex in Transport from the Early/Recycling Endosome to the Trans-Golgi Network

An in vitro transport assay, established with a modified Shiga toxin B subunit (STxB) as a marker, has proved to be useful for the study of transport from the early/recycling endosome (EE/RE) to the trans-Golgi network (TGN). Here, we modified this assay to test antibodies to all known soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) that have been shown to localize in the Golgi and found that syntaxin 5, GS28, Ykt6, and GS15 antibodies specifically inhibited STxB transport. Because syntaxin 5, GS28, Ykt6, and GS15 exist as a unique SNARE complex, our observation indicates that these four SNAREs function as a complex in EE/RE-TGN transport. The importance of GS15 in EE/RE-TGN transport was further demonstrated by a block in recombinant STxB transport in HeLa cells when GS15 expression was knocked down by its small interfering iRNA. Morphological analyses showed that some GS15 and Ykt6 were redistributed from the Golgi to the endosomes when the recycling endosome was perturbed by SNX3-overexpression, suggesting that GS15 and Ykt6 might cycle between the endosomes and the Golgi apparatus. Further studies indicated that syntaxin 5 and syntaxin 16 exerted their role in EE/RE-TGN transport in an additive manner. The kinetics of inhibition exhibited by syntaxin 16 and syntaxin 5 antibodies is similar

Identification of the bioactive components from pH-modified citrus pectin and their inhibitory effects on galectin-3 function

Citrus pectin is widely used as a gelling/thickening agent and stabilizer in the food and pharmaceutical industries. The usefulness of citrus pectin, however, has been limited due to its large size, an obstacle that can be partially overcome with ph-modified citrus pectin (mcp). In the present study, we fractionated mcp into four fractions (mcp-1, -2, -3, and -4) and then sub-fractions of type-i rhamnogalacturonan-rich pectins (rg-i: mcp-1a, mcp-2a, mcp-3sa and mcp-4a) and homogalacturonan-rich pectins (hg: mcp-2b, mcp-3sb, mcp-3p, mcp-4b). Upon analysis of their chemical structures, we found that the rg-i sub-fractions contain (1 ? 4)-linked ß-d-galactan and (1 ? 5)-linked a-l-arabinans or type-i arabinogalactan side-chains. Because parent mcp is known to inhibit hemagglutination mediated by galectin-3 (a lectin associated with cancer progression and metastasis), we used this assay to define which mcp fraction best promotes anti-galectin-3 activity. Our results demonstrate that mcp-2 was the most inhibitory with a mic of 0.06 µg/ml (ten-fold more potent than parent mcp), and that rg-i-rich pectins with (1 ? 4)-linked ß-d-galactan side-chains were more active than the other rg-i-rich and hg-rich pectins. These findings provide new insight into structure-activity relationships of mcp and provide impetus towards the development of mcp-based food stabilizers and galectin-3 targeted therapeutics for use in the clinical setting

Galectin-13, a different prototype galectin, does not bind β-galacto-sides and forms dimers via intermolecular disulfide bridges between Cys-136 and Cys-138

Abstract During pregnancy, placental protein-13 (galectin-13) is highly expressed in the placenta and fetal tissue, and less so in maternal serum that is related to pre-eclampsia. To understand galectin-13 function at the molecular level, we solved its crystal structure and discovered that its dimer is stabilized by two disulfide bridges between Cys136 and Cys138 and six hydrogen bonds involving Val135, Val137, and Gln139. Native PAGE and gel filtration demonstrate that this is not a crystallization artifact because dimers also form in solution. Our biochemical studies indicate that galectin-13 ligand binding specificity is different from that of other galectins in that it does not bind β-galactosides. This is partly explained by the presence of Arg53 rather than His53 at the bottom of the carbohydrate binding site in a position that is crucial for interactions with β-galactosides. Mutating Arg53 to histidine does not re-establish normal β-galactoside binding, but rather traps cryoprotectant glycerol molecules within the ligand binding site in crystals of the R53H mutant. Moreover, unlike most other galectins, we also found that GFP-tagged galectin-13 is localized within the nucleus of HeLa and 293 T cells. Overall, galectin-13 appears to be a new type of prototype galectin with distinct properties

RG-I-containing sugar domains from Centella Asiatica bind strongly to galectin-3 to inhibit cell–cell interactions

Abstract Background Centella Asiatica has been shown to have beneficial value for the treatment of tumors. However, its active ingredients and molecular mechanisms of action have not been fully elucidated. Pectic polysaccharides are the primary active components from medicinal plants. Moreover, these polysaccharides are regarded as potential inhibitors of galectins, such as galectin-1, -3, -7, that generally promote tumor growth. Nevertheless, detailed structural analysis of pectic polysaccharides from Centella Asiatica is sorely lacking, as is knowledge of their interactions with galectins. Methods Water-soluble pectic polysaccharides (WCAP) isolated from Centella Asiatica were purified into two homogeneous fractions (WCAP-A2b and WCAP-A5b) by a combination of anion-exchange and gel-permeation chromatography. Monosaccharide composition, FT-IR, NMR and enzymatic analyses were used to characterize their structural features. Furthermore, the interactions between galectin-1, -3, -7 and a series of these polysaccharides, including two pectin fractions and their structural domains produced by enzymatic hydrolysis, were evaluated by using hemagglutination and biolayer interferometry. Results WCAP-A2b and WCAP-A5b have weight averaged molecular weights of 30.0 kDa and 34.0 kDa, respectively, and both polysaccharides consist of rhamnogalacturonan I (RG-I), rhamnogalacturonan II (RG-II) and homogalacturonan (HG) domains, with mass ratios of 1.3: 1.0: 1.4 and 1.1: 1.0: 2.4, respectively. Their RG-I domains contain arabinan, galactan, and/or arabinogalactan, along with neutral sugar side chains that are more prevalent in WCAP-A2b than in WCAP-A5b. Hemagglutination and biolayer interferometry binding assays indicate that galectin-3 vis-à-vis galectin-1 and -7, binds strongly to the RG-I domain (likely via its neutral side chains) in WCAP-A5b, thereby inhibiting galectin-3-mediated cell–cell interactions. Conclusions Our study provides structural information on pectin polysaccharides from Centella Asiatica. Results suggest that RG-I domains from WCAP-A5b and WCAP-A2b may be developed as potential inhibitors of galectin-3-mediated cell–cell adhesion and tumor growth. Graphical Abstrac

Downregulation of miR-33a-5p in Hepatocellular Carcinoma: A Possible Mechanism for Chemotherapy Resistance.

BACKGROUND Multi-drug resistance is one of the major problems limiting the efficacy of cisplatin (CDDP) in treatment of hepatocellular carcinoma (HCC), and abnormal microRNA (miRNA) expression in drug-resistant cell lines plays an important role in liver cancer chemotherapy resistance. MATERIAL AND METHODS We established stable Hep3B and 97L HCC cell strains resistant to CDDP, both in vitro and in vivo. A combination of microRNA microarray and RT-qPCR experiments were used to screen differentially expressed miRNAs in HCC cell strains. A CCK-8 assay was carried out to detect and calculate the survival rates and relative inhibitory rates. Oligonucleotide transfection was used to confirm the regulatory function of the miRNA in HCC drug resistance. RESULTS The IC50 of Hep3B/CDDP(v), 97L/CDDP(v), Hep3B/CDDP(s), and 97L/CDDP(s) were significantly higher than that of their parental cells. Moreover, the doubling time of drug-resistant cells increased compared with their parent cells. MiRCURYTM LNA Array (v 16.0) high-throughput tests of resistant cell models and their parent cells showed that there were 5 downregulated microRNAs in the 4 drug-resistant cell lines, and we chose hsa-miR-33a-5p as our target for further study. Oligonucleotide transfection showed that miR-33a-5p overexpression increased the cisplatin sensitivity of Hep3B/CDDP(v) and 97L/CDDP(v) drug-resistant cells and reduced their resistance. Additionally, inhibition of miR-33a-5p expression reduced cisplatin sensitivity in Hep3B and 97L and increased their drug resistance. CONCLUSIONS This study confirmed that the most downregulated microRNA, miR-33a-5p, can mediate the cisplatin resistance of HCC cells, providing a new and feasible direction for research into combatting liver cancer chemotherapy resistance. Med Sci Monit 2017 Mar 14; 23:1295-1304

The Two Endocytic Pathways Mediated by the Carbohydrate Recognition Domain and Regulated by the Collagen-like Domain of Galectin-3 in Vascular Endothelial Cells

<div><p>Galectin-3 plays an important role in endothelial morphogenesis and angiogenesis. We investigated the endocytosis of galectin-3 in human vascular endothelial cells and showed that galectin-3 could associate with and internalized into the cells in a carbohydrate-dependent manner. Our work also revealed that galectin-3 was transported to the early/recycling endosomes and then partitioned into two routes – recycling back to the plasma membrane or targeting to the late endosomes/lysosomes. Various N- and C-terminal truncated forms of galectin-3 were constructed and compared with the full-length protein. These comparisons showed that the carbohydrate-recognition domain of galectin-3 was required for galectin-3 binding and endocytosis. The N-terminal half of the protein, which comprises the N-terminal leader domain and the collagen-like internal repeating domain, could not mediate binding and endocytosis alone. The collagen-like domain, although it was largely irrelevant to galectin-3 trafficking to the early/recycling endosomes, was required for targeting galectin-3 to the late endosomes/lysosomes. In contrast, the leader domain was irrelevant to both binding and intracellular trafficking. The data presented in this study correlate well with different cellular behaviors induced by the full-length and the truncated galectin-3 and provide an alternative way of understanding its angiogenic mechanisms.</p> </div

Primers.

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