The widespread use and development of aerogels for catalysis applications is due to their characteristically high surface area. However, the synthesis of typical aerogels is costly and time-consuming, and the need for supercritical drying to preserve surface area compounds both of these issues. This study serves to further modify our novel synthesis to chemically control binding sites to increase surface area. Our original synthesis involved doping fumed silica with titanyl sulfate hydrate followed by drying and calcining at high temperatures to remove any water and organic molecules. The proposed modification of this procedure involved doping fumed silica with a second, smaller compound prior to adding titanyl sulfate to chemically promote binding at sites away from naturally occurring pores in the fumed silica. Characterization through scanning electron microscopy, BET surface area analysis, and BJH pore size distribution showed that doping the fumed silica prior to adding the titanyl sulfate did result in a substantially larger surface area and an increase in nanopores. As surface area is intrinsically tied to catalysis, further developments in high surface area materials result in more efficient catalysts.
Human Immunodeficiency Virus type 1 (HIV-1) targets CD4+ cells, weakening the immune system and potentially leading to AIDS. Understanding the virus's structure and focusing on its more stable regions is essential to create more effective treatments. Genomic recognition, a highly conserved process, represents a promising drug target. Mutagenesis studies have identified the Core Encapsidation Signal (CES) as the minimal packaging unit for HIV-1, which shows nucleocapsid (NC) binding. Ding et al. determined the highest affinity binding sites of NC on the 5’ Leader of HIV are in the CES region. The central finding was that the binding of NC causes unwinding within the PSI hairpin of the viral RNA, which is important for genome packaging and viral replication. Our project focuses on the MAL over Ding's NL4-3 strain of HIV-1 to determine the binding characteristics of NC on the RNA packing signal. To quantify the number of binding sites in the MAL packaging signal and the affinity of NC on those sites, we utilized Nuclear Magnetic Resonance and Isothermal Calorimetry. Our next goal will be to characterize the RNA and Gag interactions important for nucleocapsid binding, genome selection, and selective packaging. Overall, understanding the conserved region advances HIV antiviral therapies.
Treatment for parasitic worms in animals is a common practice in veterinary medicine. Additionally, anthelmintics are a group of antiparasitic drugs that paralyze or kill the given parasite without causing any significant damage or harm to the host. This study focuses on three specific parasite preventatives commonly administered to animals which includes, Ivermectin, Albendazole, and Pyrantel. Furthermore, an N2 stain of C. elegans (microscopic worms) were utilized as models for various parasitic worms in order to gain a better understanding of how gene expression is altered when treated and exposed to varying concentrations of antihelminthic drugs. This study incorporated mixed investigations consisting of qPCR (quantitative real-time polymerase chain reaction), behavioral assays, western blots, and imaging through confocal microscopy. The scientific findings and variation in data from the results of these studies ultimately led to inconclusive results and conclusions. However, the primary purpose of these observations are to potentially elucidate resistance factors of these nematodes, which can possibly improve the effectiveness of antihelminthic drugs in actual parasitic worms.
