The Ebola virus is a highly infectious pathogen with no effective antiviral treatments currently available, prompting ongoing research into potential therapeutic options. This study evaluated the inhibitory effects of licensed non-viral drugs on Ebola virus entry and replication using bioinformatic tools. A descriptive-analytical approach was used, in which the chemical structures of selected drugs were first generated in ChemDraw Ultra 10.0 and then energy-optimized in Hyperchem 8.0. Molecular docking was performed using AutoDock4.2 to simulate interactions between the drugs and viral proteins. The analysis revealed that the interactions involved primarily hydrophobic, π-π stacking, hydrogen bonding, and cation-π interactions. Chloroquine, diphenoxylate, and amodiaquine showed the strongest binding affinity, with the most negative docking energies, indicating their potential as effective inhibitors of the GP and VP40 proteins. Conversely, erythromycin and dirithromycin, due to their high hydrophilicity, exhibited weaker binding results. Overall, the study highlighted that drugs with hydrophobic components, effective hydrogen bonding, and tertiary amines tend to show enhanced anti-Ebola properties. The bioinformatic analysis suggests that these drugs could serve as promising candidates for inhibiting Ebola virus entry and replication.
For many years, various drugs have been utilized to treat different cancer types, but some of these treatments come with adverse effects such as liver damage, hypertension, and erectile dysfunction. In the pursuit of alternative therapeutic options, several new compounds have been developed to address this clinical challenge. Yet, the interactions of these compounds with biomolecules involved in cancer development remain largely unclear. With this context in mind, the present study aimed to explore the potential theoretical interaction of a series of pyrimidinone derivatives (compounds 1-27) with the X-linked inhibitor of apoptosis protein (XIAP), a key player in cancer progression, using the Docking model. The findings indicated that certain pyrimidinone derivatives (compounds 1-6, 10, 11, 14, 15, 22-24, 26, and 27) exhibited the ability to bind with the surface of the XIAP protein. In conclusion, these results suggest that some pyrimidinone derivatives may modulate XIAP’s biological activity, making them promising candidates for cancer therapy.
Eurasian Academy of Medicine and Dentistry