Evaluation of the interactions of the Sunitinib malate with topoisomerase enzymes by in vitro enzyme and molecular docking analyses

Abstract

Today, we live with the fact that anti-cancer drugs, which are in medical use and have been identified to have many mechanisms of action, only allow the treatment of a certain number of cancer types, and despite the research of many molecules with potential anti-cancer properties, not all types of cancer can be treated. Tyrosine kinase inhibitors (TKIs) mostly destroy certain types of cancer cells and many TKIs are currently being investigated in phase stages. Determining their use for various types of cancer is especially important for cases of acquired resistance in cancer. In our study, we investigated whether Sunitinib malate molecule, a multi-target receptor tyrosine kinase inhibitor, targets the topoisomerase I enzyme in addition to its known targets. In our study, we investigated whether Sunitinib malate molecule, a multi-target receptor tyrosine kinase inhibitor, targets the topoisomerase I enzyme in addition to its known targets. The interactions of Sunitinib malate with topoisomerase enzyme I were evaluated by in vitro enzyme activity tests, and Sunitinib malate was shown to inhibit topoisomerase I enzyme in a concentration-dependent manner, and when used in combination with Camptothecin, the potential for inhibition effects was evaluated by in vitro enzyme assays and molecular docking analysis

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