We scrutinized the conventional practice of measuring an electrolyte stability window. It is shown that misleading values might be generated by this practice. Thus, we recommend that to obtain a real stability window, the working electrode material should simulate the electrodes used in a real device. Further, in applications that have a high-surface-area electrode, a new quantification of a stability window is proposed. The electrochemical stability values of various nonaqueous electrolytes that are derived this way should reflect the actual operation limits of these electrolytes in real-life devices.

No abstract

Biomaterials that mimic the extracellular matrix in both modularity and crosslinking chemistry have the potential to recapitulate the instructive signals that ultimately control cell fate. Toward this goal, modular protein polymer-based hydrogels were created through genetic engineering and enzymatic crosslinking. Animal derived tissue transglutaminase (tTG) and recombinant human transglutaminase (hTG) enzymes were used for coupling two classes of protein polymers containing either lysine or glutamine, which have the recognition substrates for enzymatic crosslinking, evenly spaced along the protein backbone. Utilizing tTG under physiological conditions, crosslinking occurred within two minutes, as determined by particle tracking microrheology. Hydrogel composition impacted the elastic storage modulus of the gel over 4-fold and also influenced microstructure and degree of swelling, but did not appreciably effect degradation by plasmin. Mouse 3T3 and primary human fibroblasts were cultured in both 2- and 3-dimensions without a decrease in cell viability and displayed spreading in 2D. The properties of these gels, which are controlled through the specific nature of the protein polymer precursors, render these gels valuable for in situ therapies. Furthermore, the modular hydrogel composition allows tailoring of mechanical and physical properties for specific tissue engineering applications.

We studied the supercooling behavior of a number of solutions of LiPF 6 in ethylene carbonate-ethyl methyl carbonate in 1:1 weight ratio with and without the presence of one of these carbons: activated carbon, carbon black, and mesocarbon microbeads. The results of our experiments of differential scanning calorimetry (DSC) show that the supercooling of less concentrated solutions is significantly diminished by the presence of a carbon, the degree and the nature of which depends on the concentration of the electrolyte and the type of carbon present. The results of our conductivity measurement also indicate precipitation in some of the electrolytes at low temperatures, which correlates well with the DSC results. We therefore conclude that the temperature range in which an electrolyte supercools without a nucleating material is unreliable for the operation of an electrochemical device containing such an electrolyte. Instead, the liquidus temperature of an electrolyte should be used as the lower limit of operation if the possibility of its crystallization is to be excluded.

Monodisperse protein polymers engineered by biosynthetic techniques are well suited to serve as a basis for creating comb-like polymer architectures for biomaterial applications. We have developed a new class of linear, cationic, random-coil protein polymers designed to act as scaffolds for multivalent display. These polymers contain evenly spaced lysine residues that allow for chemical or enzymatic conjugation of pendant functional groups. Circular dichroism (CD) spectroscopy and turbidity experiments have confirmed that these proteins have a random coil structure and are soluble up to at least 65 °C. Cell viability assays suggest these constructs are non-toxic in solution up to a concentration of 100 μM. We have successfully attached a small bioactive peptide, a peptoid-peptide hybrid, a poly(ethylene glycol) (PEG) polymer, and a fluorophore to the protein polymers by chemical or enzymatic coupling, demonstrating their suitability to serve as multivalent scaffolds in solutions or as gels.