Thermal and light-driven soft actuators based on a conductive polypyrrole nanofibers integrated poly(N-isopropylacrylamide) hydrogel with intelligent response.

The development of soft hydrogel actuators with outstanding mechanical properties, fast actuation speed, and available quantification of self-sensing actuation remains a challenging endeavor. In this work, dopamine-decorated polypyrrole nanofibers (DAPPy) were introduced into the polyethylene glycol diacrylate (PEGDA)-crosslinked poly(N-isopropyl acrylamide) network to generate a stretchable, NIR-responsive, and strain sensitive DAPPy/PNIPAM hydrogel layer. Besides, this active layer was combined with the passive ligninsulfonate sodium/polyacrylamide (LS/PAAM) to give DAPPy/PNIPAM//LS/PAAM bilayer hydrogel actuator, which exhibits ultrafast thermo-responsive actuation (19°/s) and underwater grasping and lifting performance. Moreover, the DAPPy/PNIPAM layer has excellent electrical conductivity (0.29 S/m) and thermal conversion ability (10.8 °C/min), which enable such a conductive hydrogel to act as a highly sensitive strain and temperature sensor with real-time resistance change in response to tensile strain (gauge factor up to 3.4), applied pressure, temperature, and remote NIR light irradiation. More importantly, the bilayer hydrogel actuator can integrate both actuation and self-sensing functions through the bending angle-surface temperature-relative resistance change relationship of the photothermal process. With excellent mechanical actuation and self-sensing ability, the resulting bilayer hydrogel showed a promising application potential as soft biomimetic actuating materials and soft intelligent actuators.

Lignosulfonate sodium assisted PEDOT-based all-gel supercapacitors with enhanced supercapacitance and wide temperature tolerance.

Conducting polymer hydrogels are typically employed in all-gel supercapacitors; however, Poly[3,4-ethylene-dioxythiophene] (PEDOT)-based hydrogel supercapacitors still suffer from low capacitance because of the low packing density of PEDOT in the electrodes. Here, we demonstrate lignosulfonate sodium (LS) as an excellent template to synthesize various LS-PEDOT conductive nanofillers for high mass-loading LS-PEDOT/PAAM hydrogel electrodes. Then, the optimum LS-PEDOT/PAAM electrode was assembled with a redox-active LS/PAAM/Fe3+ hydrogel electrolyte to form sandwich-structured all-gel supercapacitors, which could deliver a high specific capacitance of 672.5 mF/cm2 and an energy efficiency of 60 µWh/cm2, which are three times higher than the 220 mF/cm2 and 19.5 µWh/cm2 of the device without Fe3+ at the same condition. Such a device shows excellent temperature tolerance from -30 to 100 °C. Besides, the LS-PEDOT/PAAM electrode has excellent photothermal conversion effects under simulated solar illumination. The sluggish electrochemical performance of the SC under low temperatures could be significantly boosted by ~50 % under simulated solar light. All of these findings demonstrate that the capacitance performance of the PEDOT-based hydrogel device is successfully improved not only at room temperature but also under subzero conditions.

Nanoarmor: cytoprotection for single living cells.

Single cell modification or hybridization technology has become a popular direction in bioengineering in recent years, with applications in clean energy, environmental stewardship, and sustainable human development. Here, we draw attention to nanoarmor, a representative achievement of cytoprotection and functionalization technology. The fundamental principles of nanoarmor need to be studied with input from multiple disciplines, including biology, chemistry, and material science. In this review, we explain the role of nanoarmor and review progress in its applications. We also discuss three main challenges associated with its development: self-driving ability, heterojunction characteristics, and mineralization formation. Finally, we propose a preliminary classification system for nanoarmor.

Employing gene chip technology for monitoring and assessing soil heavy metal pollution.

Soil heavy metals pollution can cause many serious environment problems because of involving a very complex pollution process for soil health. Therefore, it is very important to explore methods that can effectively evaluate heavy metal pollution. Researchers were actively looking for new ideas and new methods for evaluating and predicting levels of soil heavy metal pollution. The study on microbial communities is one of the effective methods using gene chip technology. Gene chip technology, as a high-throughput metagenomics analysis technique, has been widely used for studying the structure and function of complex microbial communities in different polluted environments from different pollutants, including the soil polluted by heavy metals. However, there is still a lack of a systematic summarization for the polluted soil by heavy metals. This paper systematically analyzed soil heavy metals pollution via reviewing previous studies on applying gene chip technology, including single species, tolerance mechanisms, enrichment mechanisms, anticipation and evaluation of soil remediation, and multi-directional analysis. The latest gene chip technologies and corresponding application cases for discovering critical species and functional genes via analyzing microbial communities and evaluating heavy metal pollution of soil were also introduced in this paper. This article can provide scientific guidance for researchers actively investigating the soil polluted by heavy metals.

A lubricious formulation exhibiting reduced thrombogenicity, cell proliferation, and protein adsorption.

The adhesion of human platelets, erythrocytes, and leukocytes, the adsorption of protein, and the proliferation of human umbilical vein endothelial cells (HUVEC) on the surface of electropolished stainless steel and the lumen of polyurethane tubing coated with Hydromer's lubricious Duality T8B formulation was evaluated. Following exposure to a platelet-enriched suspension from citrated human whole blood, stainless steel coated with this formulation exhibited significantly reduced adhesion of platelets, erythrocytes, and granulocytes. This reduction in adhesion was confirmed using an immunohistochemical method utilizing antibodies to CD41, CD235, and CD15, respectively. The proliferation of HUVEC cells were significantly reduced when cultured on coated stainless steel. This formulation was also able to significantly reduce the adsorption of plasma proteins and the major protein in tear fluid (lysozyme) to the surface of stainless steel. The nonthrombogenic properties of Duality T8B after application to the lumen of polyurethane tubing were also examined. Following a short-term (3 h) static exposure to citrated human whole blood, microscopic examination revealed that the adhesion of platelets and erythrocytes was reduced significantly, a finding confirmed using anti-CD41 and anti-CD235 antibodies in the immunohistochemical method. A long-term (12 day) study yielded essentially identical results indicating a significant reduction in the adhesion of blood components on the luminal surface of coated polyurethane tubing. In summary, these data indicate that the application of Duality T8B onto surfaces of medical devices, such as catheters, extracorporeal circuitry, and coronary stents, could aid in reducing or preventing not only thrombus formation but also the process of restenosis.

Cell adhesion and proliferation are reduced on stainless steel coated with polysaccharide-based polymeric formulations.

Hydromer's polymeric formulations F200 and F202 were evaluated after application to a synthetic substrate for effects on cell adhesion and proliferation. A significant reduction in cell adhesion was observed when cells grown on medical-grade stainless steel coated with these polymers were stained and examined under a fluorescence microscope. This reduction in cell adhesion/proliferation was confirmed when cells were isolated and analyzed by the MTS cell proliferation assay. The rate of growth of cells on F200- and F202-coated stainless steel monitored over a period of 7 days was significantly less than that observed on uncoated stainless steel, suggesting that the rate of growth of cells was reduced. The adhesion/proliferation of human umbilical vein endothelial cells (HUVEC) to coated substrates was also decreased significantly, indicating that the reduction in cell adhesion/proliferation is not restricted to only fibroblasts. Additional studies have indicated that the adhesion/proliferation of murine fibroblasts and human endothelial cells to stainless coated with a modified formulation exhibiting a high degree of lubricity was also significantly reduced. This lubricious formulation was also observed to be effective in reducing platelet adhesion, data supporting the view that lubricity also contributes to a reduction in cell and platelet adhesion. The application of these polymeric coatings on devices designed for medical implantation may not only prevent thrombus formation but may also retard the process of restenosis.

Antithrombogenicity of Hydromer's polymeric formula F202 immobilized on polyurethane and electropolished stainless steel.

Hydromer's heparin-polymer complex (F202) was applied to polyurethane film and electropolished medical grade stainless steel. The presence of heparin on the surface was confirmed by FT-IR and immunofluorescent histochemistry. The F202 polymer was nonthrombogenic and the development of thrombi on these surfaces after exposure to recalcified human whole blood was minimal or absent. Platelet adhesion to these F202-coated surfaces, compared to control (uncoated) surfaces, was low or absent after exposure to platelet-rich plasma as determined by fluorescent staining and by immunohistochemistry. Our F202 polymer was not hemolytic after exposure to human erythrocytes and was not cytotoxic in a standard cytotoxic protocol. The F202 polymer could prove useful as an antithrombogenic coating for preventing thrombus formation on medical implants and catheters.

Metal ion activation of S-adenosylmethionine decarboxylase reflects cation charge density.

S-Adenosylmethionine decarboxylase from Escherichia coli is a pyruvoyl cofactor-containing enzyme that requires a metal cation for activity. We have found that the enzyme is activated by cations of varying charge and ionic radius, such as Li+, A13+, Tb3+, and Eu3+, as well as the divalent cations Mg2+, Mn2+, and Ca2+. All of the activating cations provide kcat values within 30-fold of one another, showing that the charge of the cation does not greatly influence the rate-limiting step for decarboxylase turnover. Cation concentrations for half-maximal activation decrease by >100-fold with each increment of increase in the cation charge, ranging from approximately 300 mM with Li+ to approximately 2 microM with trivalent lanthanide ions. The cation affinity is related to the charge/radius ratio of the ion for those ions with exchangeable first coordination sphere ligands. The exchange-inert cation Co(NH3)63+ activates in the presence of excess EDTA (and NH4+ does not activate), indicating that direct metal coordination to the protein or substrate is not required for activation. The binding of metal ions (monitored by changes in the protein tryptophan fluorescence) and enzyme activation are both cooperative with Hill coefficients as large as 4, the active site stoichiometry of this (alphabeta)4 enzyme. The Hill coefficients for Mg2+ binding and activation increase from 1 to approximately 4 as the KCl concentration increases, which is also observed with NaCl or KNO3; neither Na+ nor K+ activates the enzyme. The single tryptophan in the protein is located 16 residues from the carboxyl terminus of the pyruvoyl-containing alpha chain, in a 70-residue segment that is not present in metal ion independent AdoMet decarboxylases from other organisms. The results are consistent with allosteric metal ion activation of the enzyme, congruent with the role of the putrescine activator of the mammalian AdoMet decarboxylase.

Catalytic properties of the archaeal S-adenosylmethionine decarboxylase from Methanococcus jannaschii.

S-Adenosylmethionine decarboxylase (AdoMetDC) is a pyruvoyl cofactor-dependent enzyme that participates in polyamine biosynthesis. AdoMetDC from the Archaea Methanococcus jannaschii is a prototype for a recently discovered class that is not homologous to the eucaryotic enzymes or to a distinct group of microbial enzymes. M. jannaschii AdoMetDC has a Km of 95 microm and the turnover number (kcat) of 0.0075 s(-1) at pH 7.5 and 22 degrees C. The turnover number increased approximately 38-fold at a more physiological temperature of 80 degrees C. AdoMetDC was inactivated by treatment with the imine reductant NaCNBH3 only in the presence of substrate. Mass spectrometry of the inactivated protein showed modification solely of the pyruvoyl-containing subunit, with a mass increase corresponding to reduction of a Schiff base adduct with decarboxylated AdoMet. The presteady state time course of the AdoMetDC reaction revealed a burst of product formation; thus, a step after CO2 formation is rate-limiting in turnover. Comparable D2O kinetic isotope effects of were seen on the first turnover (1.9) and on kcat/Km (1.6); there was not a significant D2O isotope effect on kcat, suggesting that product release is rate-limiting in turnover. The pH dependence of the steady state rate showed participation of acid and basic groups with pK values of 5.3 and 8.2 for kcat and 6.5 and 8.3 for kcat/Km, respectively. The competitive inhibitor methylglyoxal bis(guanylhydrazone) binds at a single site per (alphabeta) heterodimer. UV spectroscopic studies show that methylglyoxal bis(guanylhydrazone) binds as the dication with a 23 microm dissociation constant. Studies with substrate analogs show a high specificity for AdoMet.

Methylthioadenosine phosphorylase regulates ornithine decarboxylase by production of downstream metabolites.

The gene encoding methylthioadenosine phosphorylase (MTAP), the initial enzyme in the methionine salvage pathway, is deleted in a variety of human tumors and acts as a tumor suppressor gene in cell culture (Christopher, S. A., Diegelman, P., Porter, C. W., and Kruger, W. D. (2002) Cancer Res. 62, 6639-6644). Overexpression of the polyamine biosynthetic enzyme ornithine decarboxylase (ODC) is frequently observed in tumors and has been shown to be tumorigenic in vitro and in vivo. In this paper, we demonstrate a novel regulatory pathway in which the methionine salvage pathway products inhibit ODC activity. We show that in Saccharomyces cerevisiae the MEU1 gene encodes MTAP and that Meu1delta cells have an 8-fold increase in ODC activity, resulting in large elevations in polyamine pools. Mutations in putative salvage pathway genes downstream of MTAP also cause elevated ODC activity and elevated polyamines. The addition of the penultimate salvage pathway compound 4-methylthio-2-oxobutanoic acid represses ODC levels in both MTAP-deleted yeast and human tumor cell lines, indicating that 4-methylthio-2-oxobutanoic acid acts as a negative regulator of polyamine biosynthesis. Expression of MTAP in MTAP-deleted MCF-7 breast adenocarcinoma cells results in a significant reduction of ODC activity and reduction in polyamine levels. Taken together, our results show that products of the methionine salvage pathway regulate polyamine biosynthesis and suggest that MTAP deletion may lead to ODC activation in human tumors.

Enzymatic properties of S-adenosylmethionine synthetase from the archaeon Methanococcus jannaschii.

S-Adenosylmethionine synthetase (ATP:l-methionine S-adenosyltransferase, MAT) catalyzes a unique enzymatic reaction that leads to formation of the primary biological alkylating agent. MAT from the hyperthermophilic archaeon Methanococcus jannaschii (MjMAT) is a prototype of the newly discovered archaeal class of MAT proteins that are nearly unrecognizable in sequence when compared with the class that encompasses both the eucaryal and bacterial enzymes. In this study the functional properties of purified recombinant MjMAT have been evaluated. The products of the reaction are AdoMet, PP(i), and P(i); >90% of the P(i) originates from the gamma-phosphoryl group of ATP. The circular dichroism spectrum of the dimeric MjMAT indicates that the secondary structure is more helical than the Escherichia coli counterpart (EcMAT), suggesting a different protein topology. The steady state kinetic mechanism is sequential, with random addition of ATP and methionine; AdoMet is the first product released, followed by release of PP(i) and P(i). The substrate specificity differs remarkably from the previously characterized MATs; the nucleotide binding site has a very broad tolerance of alterations in the adenosine moiety. MjMAT has activity at 70 degrees C comparable with that of EcMAT at 37 degrees C, consistent with the higher temperature habitat of M. jannaschii. The activation energy for AdoMet formation is larger than that for the E. coli MAT-catalyzed reaction, in accord with the notion that enzymes from thermophilic organisms are often more rigid than their mesophilic counterparts. The broad substrate tolerance of this enzyme proffers routes to preparation of novel AdoMet analogs.