In silico analysis of Coenzyme Q10 interaction with the heme-hemoglobin complex: Implications for oxidative stress and inflammation in severe malaria

Plasmodium falciparum , the primary causative agent of severe malaria, catabolizes hemoglobin to obtain nutrients, resulting in the accumulation of toxic free heme. To mitigate this toxicity, the parasite converts heme into inert hemozoin. Chloroquine inhibits this detoxification process, leading to the buildup of free heme and exacerbating oxidative stress. Recent studies suggest that Coenzyme Q10 (CoQ10) may counteract malaria-induced oxidative stress and inflammation. However, its molecular interactions with key biomolecules remain unclear. This study aims to evaluate the potential molecular interactions of Coenzyme Q10 with heme and hemoglobin using an in silico approach. The study involved molecular docking of Coenzyme Q10 on heme- hemoglobin, ADMET studies of Coenzyme Q10 and molecular dynamic simulations of Coenzyme Q10-heme-hemoglobin complex. Coenzyme Q10 has favorable ADMET properties and positively interacts with the heme group and some amino acids of the hemoglobin, forming a stable complex, though its ADMET profile presents challenges such as poor solubility. These findings demonstrate that Coenzyme Q10 can reduce the degradation of hemoglobin via direct interaction, subsequently regulating heme build-up. This study identifies potential molecular interactions between Coenzyme Q10 and heme–hemoglobin complexes based on computational analyses, providing molecular-level insights which may infer functional or therapeutic outcomes.