Leukaemia is a type of cancer characterized by an increased proliferation of immature white blood cells. Each year, 350000 people worldwide are diagnosed with leukaemia leading to 250000 deaths per annum. As current treatments for leukaemia lack specificity and result in many undesirable side effects and resistance, there is a need for new therapies that target cancer cells selectively. 14-3-3ζ is a dimeric protein that binds to client proteins in cells regulating their function. It is overexpressed in leukaemia and is involved in many signalling processes that promote tumour initiation and progression. Increased 14-3-3ζ expression has been shown to lead to chemotherapeutic and radiotherapy resistance. Thus, 14-3-3ζ is a potential target for anti-cancer drug development. Current 14-3-3ζ inhibitor classes use a conventional approach whereby they target the client protein binding site. However, these compounds require strong binding affinities and high concentrations in order to outcompete physiological substrates. The dimeric structure of 14-3-3 is essential for its function and studies have shown that disrupting 14-3-3 dimers reduces its anti-apoptotic activity. Hence, this project aims to discover the binding mechanism of a new class of anti-cancer agents that target the 14-3-3 dimer interface, in order to destabilize it leading to disruption of its anti-apoptotic function. The characterization of these new class of compounds to the binding site of 14-3-3ζ dimer interface is being done through computational docking, crystallography, and biophysical techniques. This work will provide the basis for developing novel therapeutic strategies to inhibit 14-3-3 as a treatment for leukaemia.