Tuberculosis (TB) is a disease mostly caused by Mycobacterium tuberculosis (MT) that primarily affects the lungs and it is estimated that TB causes around 2 million deaths globally each year. The impact of TB is worsened due to the emergence of multidrug resistant MT making the discovery of new effective antibiotics a priority. One thing that sets MT apart from other bacteria is the way it links the peptidoglycan layer in the cellular wall together, peptidoglycan gives the cellular wall rigidity and is important for the bacteria to maintain physiological functions. While most bacteria use the D,D-transpeptidase enzymes to link the peptidoglycan layers, MT uses the L,D-transpeptidase enzymes and specifically the L,D-transpeptidase 2 which produces 80 % of these links. The L,D-transpeptidase 2 has a different amino acid in the active site making it a valid target for the antibiotic faropenem. Faropenem binds to the enzyme irreversibly where it splits into two fragments leaving a smaller fragment that disables the enzyme and killing the bacteria. By designing and synthesising analogues to faropenem, the effectiveness of similar substances is investigated. This project has identified two different ways that analogues can be designed. By oxidising faropenem, a more stable fragment that is bound to the enzyme may be formed. another way is by changing the sulphur to another heteroatom in faropenems 5-ring, resulting in a more stable leaving fragment which may increase its effectiveness. Several oxidising methods were investigated but none of them resulted in a stable product that could be isolated.