Characterization of the metallo-ß-lactamase from Pseudomonas aeruginosa, IMP-1.

The rate at which pathogenic bacteria are gaining antibiotic resistance has become increasingly alarming. Major contributors of this antibiotic resistance in microbes are a class of enzymes known as β-lactamases. These enzymes are effective in breaking down the most commonly prescribed antibiotics at present. This work investigates two separate metallo-β-lactamase enzymes, first IMP-1, which provides antibiotic resistance to Pseudomonas aeruginosa, and second Bla2, which grants antibiotic resistance to Bacillus anthracis. The main focus of this work was to investigate and characterize IMP-1 according to its activity and stability in temperature and pH. This was done in an effort to increase the general knowledge for potential inhibitors to be designed. The secondary focus of this work was to examine the ability of novel hydroxamate compounds to inhibit the growth of bacterial cells expressing Bla2. In addition to this work, aptamers were investigated as a potential means of future inhibitor design.