Design and synthesis of peptides from bacterial ParE toxin as inhibitors of topoisomerases

► Twelve linear peptides derived from E. coli ParE protein were synthesized. ► Four of the twelve peptides behaved as good bacterial topoisomerases inhibitors. ► ParELC10 was the most potent inhibitor for both DNA gyrase and topoisomerase IV. ► A structural change in ParELC10 resulted in a less active peptide, but with inhibitory activity on human topoisomerase II.