biostudies-literature00460Nepomuceno GMNational Institute of Allergy and Infectious DiseasesConselho Nacional de Desenvolvimento Científico e TecnológicoAlfred P. Sloan FoundationArnold and Mabel Beckman FoundationU.S. Department of Education308-12https://www.ebi.ac.uk/biostudies/studies/S-EPMC4360151biostudies-literatureUnknown6(3)The bacterial cell division protein FtsZ is one of many potential targets for the development of novel antibiotics. Recently, zantrin Z3 was shown to be a cross-species inhibitor of FtsZ; however, its specific interactions with the protein are still unknown. Herein we report the synthesis of analogues that contain a more tractable core structure and an analogue with single-digit micromolar inhibition of FtsZ's GTPase activity, which represents the most potent inhibitor of Escherichia coli FtsZ reported to date. In addition, the zantrin Z3 core has been converted to two potential photo-cross-linking reagents for proteomic studies that could shed light on the molecular interactions between FtsZ and molecules related to zantrin Z3.ACS medicinal chemistry lettersSynthesis and Evaluation of Quinazolines as Inhibitors of the Bacterial Cell Division Protein FtsZ.PMC4360151R01AI08093-04S1R01AI08093Pollo LAMoore JTTadeus CAmes JBSarabia FJChan KMYao ZShaw JTMartin KSAnderson DEHuynh VNepomuceno GMO'Brien TE46falseSynthesis and Evaluation of Quinazolines as Inhibitors of the Bacterial Cell Division Protein FtsZ.The bacterial cell division protein FtsZ is one of many potential targets for the development of novel antibiotics. Recently, zantrin Z3 was shown to be a cross-species inhibitor of FtsZ; however, its specific interactions with the protein are still unknown. Herein we report the synthesis of analogues that contain a more tractable core structure and an analogue with single-digit micromolar inhibition of FtsZ's GTPase activity, which represents the most potent inhibitor of Escherichia coli FtsZ reported to date. In addition, the zantrin Z3 core has been converted to two potential photo-cross-linking reagents for proteomic studies that could shed light on the molecular interactions between FtsZ and molecules related to zantrin Z3.2015-01-01T00:00:00Z2015 Mar2024-11-09T10:53:24.006Z2019-03-27T01:48:12ZS-EPMC43601512581515110.1021/ml500497s