Molecular docking studies of Daunorubicin-Histone H1 Interactions

This study investigates the interaction between the anthracycline antibiotic daunorubicin and histone H1, a key chromosomal protein, shedding light on the potential involvement of chromatin components in drug-chromatin interactions and their role in anthracycline-mediated tumor cell toxicity. Using molecular docking, the study explores the binding affinity of daunorubicin to histone H1, providing atomic-scale details of the interaction. The results indicate a binding affinity between daunorubicin and histone H1, suggesting the potential role of histones in the action of this antibiotic. The study identifies specific residues in histone H1 that are in close proximity to the daunorubicin ligand, revealing insights into the molecular details of the interaction. Multiple binding pockets for daunorubicin within the three-dimensional structure of the histone H1-doxorubicin interaction are also identified, suggesting histone H1 as a potential target for this anticancer drug. Additionally, the study finds that van der Waals forces predominantly govern the histone H1-daunorubicin interaction, with no significant contribution from electrostatic forces. The calculated Gibbs free energy underscores the potential significance of histone H1-daunorubicin interactions in drug toxicity within tumor cells. These insights into the mode of action of anthracyclines and the role of histones in tumor cell toxicity may have implications for the development of novel therapeutic strategies targeting chromatin components, providing valuable information for understanding the molecular mechanisms underlying anthracycline activity and its implications for cancer therapy.