Comparative Investigation on Interaction of Potent Antimalarials with Human Serum Albumin via Multispectroscopic and Computational Approaches.

In this study, comparative investigation was done to explore the interaction mechanisms between two potential antimalarial compounds, JMI 346 and JMI 105, and human serum albumin (HSA), a vital carrier protein responsible for maintaining crucial biological functions. Our objective was to assess the pharmacological efficiency of these compounds while comprehensively analyzing their impact on the dynamic behavior and overall stability of the protein. A comprehensive array of multispectroscopic techniques, including UV-VIS, steady state, synchronous, 3D fluorescence and CD spectroscopy, docking studies and molecular dynamics (MD) simulations, were performed to probe the intricate details of the interaction between the compounds and HSA. Our results revealed that both JMI 346 and JMI 105 displayed promising pharmacological effectiveness within the context of malaria therapy. However, JMI 346 was found to exhibit a significantly higher affinity and only minor altered impact towards HSA, suggesting a more favorable interaction with the protein on the dynamic behavior and overall stability of the protein in comparison to JMI 105. Further studies can build upon these results to optimize the drug-protein interaction and enable the development of more potent and targeted antimalarial treatments.