Persisters are a small portion of a cellular population with heterogenous phenotypes, that switch to a dormant, growth arrested state upon antibiotic exposure allowing them to survive. Antibiotic persistence is a growing field of interest due to the recalcitrance of infection presenting a challenge to antibiotic therapy. Type II toxin-antitoxin systems have been implicated in persister cell formation. The TacT family of toxins containing a Gcn5 N-acetyltransferase fold have been identified to contribute to persistence in Salmonella enterica. Identifying pan peptide inhibitors of the TacT toxin family is a potential method to prevent the formation of persister cells in Salmonella Typhimurium and Salmonella Enteritidis. Towards this long-term goal, characterisation of the TacT interactions with their respective antitoxins has been reported in this thesis. Toxin-antitoxin affinities have been identified to be within the nanomolar to picomolar range, with a biphasic relationship observed. The protein-protein interaction demonstrated a high salt dependence suggesting primarily electrostatic interactions are involved. The results provide a starting point for the identification of a peptide compound to treat persistence by targeting the TacT toxins. In parallel this thesis reports the trial expression of the wild-type TacT proteins. This is crucial for the accurate characterisation of the proteins and for activity assays.