Experimental screening for bacterial cell division inhibitors among natural extracts and synthetic compounds, identified FtsZ binding ligands with bacterial inhibitory activities at the low µM range . The bacterial inhibition activities of a limited set of ligands correlated better with their idc/nbd bindingaffinities than with other experimental assays including inhibition of FtsZ polymerization or regeneration of GTPase activity 10, 11 . Therefore, screening for improved binding to FtsZ may be the best strategy to predict antibacterial activity, as recently suggested . The reference anti-staphylococcal PC190723 inhibitor that binds idc at the FtsZ open-tense conformation at low µM ranges was identified by in vitro assaying benzamide derivatives 15 12, 16 . PC190723 contains a difluorobenzamide moiety bound to diheterorings. PC190723 stabilizes the FtsZ filament as suggested by the cocrystalized structure 17, 18 . at low µM ranges However, neither PC190723 nor its varied benzamide analogs became clinically used in medicine, because of pharmacological problems, the generation of bacterial FtsZ gene resistant mutations 9, 19 , and despite been tested in combination with other drugs with some success . The PC190723-derived TXA709, TXA436, TXA541 and TXH9179 drugs and prodrugs (Taxis pharmaceuticals, Monmouth Junction, Nj, USA)