Date of Award


Document Type

Undergraduate Thesis

Degree Name




Faculty Mentor

David C. Forbes


The overexpression of protein phosphatase 5 has been correlated to tumor cell reproduction making it a candidate for small molecule drug therapy. Selective and potent inhibition of protein phosphatase 2A (PP2A) enzyme has been previously achieved through the development of the molecule fostriecin with key functionality being a lactone and unsaturated linear chain. The large synthetic overhead of fostriecin has led to exploration of other small molecule inhibitors that could mirror fostriecin’s interaction with the active site in the catalytic domain of PP5. The naturally occurring inhibitor, cantharidin, is functionalized with an epoxy containing eleven carbon chain to optimize binding with the active site of PP5 and to promote selectivity and potency through unique interactions with the amino acid residues. The stereoisomers formed in the Diels-Alder reaction between the robust dienophile N-phenylmaleimide and furfuryl alcohol are isolated and identified. The biologically active exo confirmation is selectively recrystallized and employed in further synthetic steps with the final product tested for inhibitory action against the PP5 enzyme.