The　p28　peptide,　derived　from　the　blue　copper　protein　azurin,　is　known　to　enhance　the　anticancer　capabilities　of　the　tumor　suppressor　p53　likely　binding　to　its　DNA-binding　domain　(DBD).　The　p28-p53　DBD　complex　has　been　investigated　by　steered　molecular　dynamics　in　order　to　characterize　the　unbinding　process　at　atomic　resolution.　We　found　that　the　unbinding　of　the　complex　follows　a　candidate　pathway　with　a　well-defined　detaching　sequence　between　the　partners.　The　analysis　of　the　unbinding　force　and　the　calculation　of　the　irreversible　work　done　along　several　unbinding　paths　have　allowed　us　to　extract　information　on　the　energy　landscape　regulating　the　unbinding　process.