Don’t miss your opportunity to be a part of this event, now a highly anticipated Campbell tradition, a decade in the making! More information at: library.campbell.edu/symposium2020
A fundamental goal of supramolecular chemistry is the control of forces between groups of molecules in the formation of nanostructures. These structures often are not strong enough to resist changes in environmental factors and chemical attack. In this research, a cyanine dye monomer known for its ability to form metastable nanotubes will be modified to create a monomer capable of creating a polymerized diacetylene backbone to form a stronger nanostructure. The synthetic procedure has been planned in such a manner as to prioritize safety and to minimize cost. Progress has been achieved in conducting this synthesis and will be presented.
Countries within the developing world have limited capabilities to regulate the quality of medications sold there. At the University of Notre Dame, the Distributed Pharmaceutical Analysis Lab was formed to test these medications in collaboration with other US undergraduate institutions. Through this partnership, a liquid chromatography assay was designed through a comparative implementation of the United States Pharmacopeia methodology for albendazole, an anthelmintic medication. To support this assay, multiple system suitability tests are being performed to ensure the validity of the process. This poster will outline this project’s obstacles and, ultimately, how they are currently being resolved.
Enzymes are attractive catalysts for organic synthesis because they function under mild conditions and can provide high stereoselectivity. Unfortunately, the use of enzymes for synthesis is limited by the number of reactions that have no enzymatic counterpart. This can be remedied by taking advantage of promiscuous activity of enzymes in synthetic reactions. For example, thiamine-dependent enzymes have been used to produce non-natural α-hydroxyketones. Our goal is to perform an enzymatic dynamic kinetic resolution to produce these valuable products with high yield and stereoselectivity. We have synthesized substrates and cloned the enzyme, with characterization of the enzyme in the reactions forthcoming.
Thiamine diphosphate-dependent enzymes have been explored for their ability to produce alpha-hydroxy ketones with high levels of enantioselectivity. Less explored, however, is the ability of these enzymes to control the configuration about multiple chiral centers. This project focuses on developing an enzymatic dynamic kinetic resolution of racemic substrates to produce alpha-hydroxy ketones with high enantio- and diastereoselectivity and high yield. We have successfully synthesized the substrates, with characterization of the enzymes in these reactions forthcoming. This work will provide an efficient and green approach to synthesize valuable alpha-hydroxy ketone products as precursors to pharmaceuticals and other important molecules.
