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Topoisomerase inhibitors act on the enzymes that cut and rejoin DNA strands to relieve torsional stress. Type I topoisomerases cleave a single DNA strand, while type II enzymes pass one double helix through a transient break in another. Many inhibitors stabilize the cleavage complex, in which the enzyme remains covalently attached to broken DNA. Camptothecin traps topoisomerase I in this way and produces protein-linked DNA breaks. Irinotecan and its active metabolite SN 38 are camptothecin derivatives with the same target. Etoposide, doxorubicin and ellipticine inhibit topoisomerase II and are used in DNA damage and cell death research. Moxifloxacin, a fluoroquinolone antibacterial, represents the inhibitors of bacterial type II topoisomerases.
