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  • Structure-based discovery of novel inhibitors of human topoisomerase ▫$II \alpha$▫
    Pogorelčnik, Barbara, 1985- ...
    DNA topoisomerases comprise a large family of enzymes that catalyse topological changes in DNA. These enzymes perform their functions by creatingtransient double-stranded breaks in the DNA molecule ... in order to allow another DNA molecule pass through the break. Due to their role in inducing topological changes, DNA topoisomerases represent one of the important targets for cancer chemotherapy. Human topoisomerase Ha is a homodimer macromolecule, which consists of three domains and has a close homology with bacterial the DNA gyrase. Topoisomerase II targeting agents areclassified into two major groups that differ in their mechanism of action.First, a more established group of molecules are named poisons, due totheir role in stabilization of the covalent cleavage complex and conversion of this enzyme into a cellular toxin which is lethal to normal cells. The second group are designated as catalytic inhibitors, and differ from poisons since they do not stabilize the covalent cleavage complex, but interfere in other steps of the described catalytic cycle. DNA topoisomerase II is a well-established and validated target for development of novel antitumor agents. The aim of our research was to identify novel inhibitors that bind to human A TPase domain and thus blocking binding of A TP molecule. Starting from available structural information we identified a novel series of purine-based inhibitors of topoisomerase IIa by implementing structure-based design procedure. This novel class of DNA topoisomerase IIa inhibitors was further investigated by surface plasmonic resonance.
    Vir: 2nd Meeting of the Paul Ehrlich MedChem Euro-PhD Network : 9th - 11th September 2012, Ljubljana, Slovenia : [book of abstracts] (Str. 76)
    Vrsta gradiva - prispevek na konferenci
    Leto - 2012
    Jezik - angleški
    COBISS.SI-ID - 5108506

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