Repurposing Drugs: Unraveling Anti-Cancer Interactions with the Kinase Domain of Human HER2

06 December 2023, Version 1
This content is a preprint and has not undergone peer review at the time of posting.


Human epidermal growth factor receptor 2 (HER2) is a transmembrane tyrosine kinase receptor that is overexpressed in many types of cancer, including breast cancer. HER2 overexpression is associated with poor prognosis and resistance to therapy. Therefore, HER2 is a promising target for cancer therapy. In this study, we investigated the binding and stability of a number of drugs with the kinase domain of HER2 using computational docking and molecular dynamics simulations. The drugs included oxycodone, methylamino luvinilate, ciclesonide, salicylic acid, melphalan, ibuprofen, N-acetyl tyrosine, and aspirin. All drugs except phenylalanine and methylamino luvinilate docked with HER2 and formed stable complexes. The molecular dynamics simulations showed that the drug-HER2 complexes remained stable throughout the simulation time of 100 ns. The drugs interacted with HER2 through a variety of interactions, including hydrogen bonding, hydrophobic interactions, and electrostatic interactions. The results of this study suggest that these drugs could be potential candidates for HER2-targeted cancer therapy. However, further in vitro and in vivo studies are needed to validate these findings.


computational chemistry
breast cancer
drug repurposing


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