Background:In todays world, its becoming increasingly difficult to ignore the role of cancer in social health. Breast cancer remains the second global cause of death in women. Alterations disrupt normal cell function, cause cancerous cells to over-proliferate, and avoid mechanisms that might typically control their growth, division, and migration. A disruption in signalling pathways, a mutation that might lead to overexpression of certain genes that can, in turn, activate the signalling pathway and send it into an override mode that leads to diseases such as cancers. These signalling pathways can be targeted not only for use as biomarkers for the early detection of certain cancers but also for targeted treatment of cancers. The prospect of the development of new substances with antitumoral potential is of great importance for thetreatment of breast cancer. Result:The objective of this work is to design a peptide from a laboratory-produced Protease enzyme isolated from Bacillus cereus HNand use that as a drug or ligand that could potentially bind to the LRP5 protein and inactivate the Wntsignalling pathway in triple-negative breast cancer cells. Conclusion:The work was aimed at computational modelling of a safe peptide which followed the pharmacokinetic parameters and conducting docking analysis to assess the binding free energy between LRP 5 and the designed peptide. The docking results show that the ligand is a good candidate for novel drug development. The models created and analysed in this work will most certainly help in future research on targeting the Wntsignalling pathway and its components.