Less than 50% of patients with invasive neuroblastoma who have MYCN gene overexpression survive, and recurrence rates are incredibly high. . Thus, focusing on the MYCN protein may be crucial for treating cancer . However, due to the complex structure of MYCN focusing on manipulating the proteins that interact with MYCN to indirectly regulate it can be an alternative strategy . BRD4 is one of the proteins that controls the MYCN activation by binding to a specific site of DNA and inhibiting BRD4 can directly affect the MYCN activation mitigating neuroblastoma . PROTACs bring the cancer suppressing E3 ubiquitin ligase in close proximity with BRD4 protein which allows for the degradation of the BRD4 protein . THE E3 ligase ubiquitin inhibits BRD4 protein activity . Recently, Jia. et al. have developed PROTACs against neuroblastoma inducing BRD4 proteins which are eventually degraded by the E3 ligase protein . We hypothesize that the aptamers used in this study will interact strongly at the interface between the BRD4 and E3 ligase protein. The current investigation explores the identification of inhibitors that can bind to both proteins (BRD4 and E3 ligase) and could help in the ubiquitination of the BED4 leading to its proteasomal degradation. In particular, we have investigated the interactions of these molecules through molecular docking simulations. PROTACs to the BRD4-L3 ligase protein. Moreover, mutations were performed in the PROTACs structure to enhance their binding affinity. This research will aid in the design of PROTACs that exerts potent anticancer effects against neuroblastoma.