The structural insights obtained from the cryogenic electron microscopy structures of M. tuberculosis ATP synthase with BDQ and TBAJ-587 bound, as well as human ATP synthase bound to BDQ, provide a detailed understanding of the binding interactions between these compounds and the enzyme subunits. By analyzing the specific regions where BDQ and TBAJ-587 interact with the ATP synthase subunits in both M. tuberculosis and human enzymes, researchers can identify key structural differences that can be exploited for designing more selective diarylquinoline compounds. By focusing on modifying the chemical structure of the compounds to target unique binding sites or alter specific functional groups that are crucial for inhibiting human ATP synthase while maintaining efficacy against M. tuberculosis ATP synthase, it is possible to develop novel compounds with improved selectivity and reduced off-target effects on human enzymes.