Next-generation energy storage materials aim to combine the best characteristics of batteries and supercapacitors, producing devices that concurrently deliver high energy and power densities. In order to achieve this goal, the kinetics of ion and electron transport within the electrodes must be enhanced while maintaining a large volume fraction of electrolytically active material for energy storage. In this regard, the idealized electrode microstructure has been envisioned as a three-dimensional, co-continuous arrangement of percolating domains that allow for large interfacial contact between the constituent phases and low-resistance paths for ion and electron transport. In this dissertation, I report a novel method to produce this unique microstructure through the use of soft matter templates derived from bicontinuous interfacially jammed emulsion gels (bijels). These non-equilibrium soft materials inherently have a co-continuous microstructure, where two interpenetrating fluid domains are kinetically arrested through jamming of particles at the fluid-fluid interface during spinodal decomposition. The neutrally-wetting colloids adsorb to the fluid interface upon phase separation and become jammed when the interfacial area is sufficiently reduced to just accommodate them. The characteristic domain size, which establishes both the pore diameter and the internal surface area, is controlled solely through the overall colloid volume fraction and can be tuned over a wide range. Through simple chemical post processing steps, bijels are converted to electrolytically active composites. Combined, the morphological control afforded during bijel formation and our chemical processing steps allow for independent tailoring of the microstructural parameters that govern the electrode’s electrochemical performance. In this work, I present composite electrodes that I have synthesized through this route and demonstrate how their salient electrochemical characteristics are dictated by these morphological parameters, allowing for concurrent delivery of high energy and power, bridging the gap between modern batteries and supercapacitors.

Type I interferons (IFN-I) are a highly evolutionarily conserved class of cytokines that are an essential defense against viral infection in vertebrates. However, prolonged or excessive IFN-I can be detrimental for the host. IFN-I can be deleterious in bacterial infections, including infections by major bacterial pathogens such as Mycobacterium tuberculosis, and can drive autoimmunity. The mechanisms that critically restrain inappropriate IFN-I induction are not well understood. We found a novel role for repression of IFN-I transcription by SP140, an immune-cell specific epigenetic reader that forms nuclear bodies. SP140 is also highly conserved in vertebrates, but the functions and mechanisms of action of SP140 and related proteins are still unknown. We found that Sp140–/– mice are highly susceptible to bacterial infections due to modest overproduction of IFN-I. We set out to characterize the mechanism by which SP140 represses IFN-I to further elucidate the functions of this understudied epigenetic reader and mechanisms of negative regulation of IFN-I. We profiled the genes bound and transcriptionally regulated by SP140, and found that SP140 binds and represses the transcription of the mouse homologs (Gm21188/Gm36079) of a mysterious human gene called the annexin II receptor (ANXA2R). GM36079 promote IFN-I transcript stability in the absence of SP140 by binding and presumably inhibiting the major messenger RNA deadenylase complex CCR4-NOT, leading to elevated and sustained levels of IFN-I transcript in Sp140–/– macrophages at late timepoints after induction of IFN-I. As IFN-I promotion appears to be a major function of the protein encoded by Gm21188/Gm36079, we name these genes Resist1 and Resist2, which encode the protein RESIST (REgulated Stimulator of Interferon via Stabilization of Transcript). Mechanistically, the repression of IFN-I by SP140 required DNA-binding and histone mark recognition domains, as well as an oligomerization domain responsible for nuclear body formation. SP140-mediated repression of IFN-I may allow the host to counter viral disruption of nuclear bodies. Nuclear bodies are large multiprotein complexes within the nucleus that can mediate numerous processes including transcription and DNA damage repair, but also antiviral defense by suppressing the transcription of viral genomes in the nucleus. We found that, like the SP140-like antiviral protein SP100, SP140 repressed replication of the murine gammaherpesvirus MHV68. The antiviral activity of SP140 suggests that SP140-mediated repression of IFN-I may allow SP140 to “guard” itself. Disruption of SP140 nuclear bodies by viral effectors may unleash elevated IFN-I through RESIST-mediated IFN-1 transcript stabilization, thus allowing the host to counter viral replication and viral targeting of antiviral nuclear bodies. Intriguingly, we also found a novel role in IFN-I transcriptional repression in macrophages by murine SP100, although this mechanism appears to be distinct from the mechanism by which SP140 inhibits IFN-I. Similar to SP140, SP100 has been shown to be targeted by viral effectors, although its role in gene regulation of the host is entirely unknown. As SP100 is intrinsically antiviral, SP100-mediated repression of IFN-I suggests that SP100, at least in mice, “guards” itself from degradation by viral effectors. The repression of IFN-I by the nuclear bodies SP140 and SP100 demonstrate an elegant multilayered defense strategy against viral infection employed by the host in the battle for the nucleus. Our work adds to the understanding of negative regulation of IFN-I, which is an essential antiviral innate immune defense in vertebrates. Our results suggest a novel and important function for the annexin II receptor, which is understudied, in regulation of IFN-I. Similarly, our work sheds further light on how the highly conserved SP140-like proteins function. As regulation of IFN-I is central to diverse outcomes in disease ranging from autoimmunity, to cancer, to bacterial infections, our work identifies new points of potential dysregulation or possible therapeutic modulation of IFN-I in human disease. Similarly, the SP140-like proteins play important roles in innate immune defense against pathogens and in human immune disorders, and contain domains that are druggable. Characterizing the functions and mechanisms of actions of these proteins may provide valuable information on the etiology of human immune disorders associated with the SP140-like proteins, and highlight novel therapeutic opportunities for modulation of immune responses, including but potentially not limited to IFN-I.