Timothy Miller University of Evansville
Faculty Sponsor(s): Roslyn Lampkins University of EvansvilleThis work shows the design, synthesis, and characterization of a purine derived molecule with characteristics tailored to target gram-negative bacteria. This molecule has a rigid, flat, and polar design that will allow it to enter the bacterium by penetrating its two cell membranes and porin protein channels. Once inside the bacterium, molecular recognition design features will allow this agent to strategically bind to the ATP binding site of the DNA gyrase enzyme (GyrB), a target that has been successfully less explored than the “cleavage/ligation” active site of the DNA gyrase enzyme. This binding is expected to inhibit the enzyme’s biological activity of replicating bacterial DNA by essentially cutting off its ATP fueled energy supply, which will lead to the bacteria’s inability to divide and replicate, ultimately resulting in the death of the cell.
When & Where
Irwin Library 1st Floor