Nootshy Romage

Conducted Research on HMG1 (High Mobility Group Box 1). HMGB1 is a nuclear protein that acts as a transcription factor and cell growth factor. extracellularly it acts as a proinflammatory cytokine that is a mediator of lethal systemic inflammation. It is released by activated macrophages. The binding of HMGB1 to the TLR4 sensory receptor along with MD-2 causes the release of proinflammatory cytokines. The accumulation of these cytokines can be detrimental to an organism. Therefore, I conducted research on HMGB1 with a new azatide peptidomimetic version of its original peptide to observe its activity. This new Peptide is supposed to inhibit its function by blocking its function to induce the secretion of proinflammatory cytokines. This was tested on murine macrophages and analyzed using the sandwich ELISA techniques and more.

Studying how bacteria communicate with each other is crucial to developing new ways to combat the unwanted presence of these organisms. A molecule implicated in the signaling pathway for the formation of biofilms in bacteria is monapterin. Our goal is to develop a high-yielding synthesis of monapterin. This molecule is difficult to obtain monapterin or its derivatives. Thus far, we have proposed a six-step synthesis of monapterin. If successful this molecule has great potential to be used in biology research and more.