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Iron(II) Supramolecular Helicates Condense Plasmid DNA and Inhibit Vital DNA‐Related Enzymatic Activities
Authors:Dr Jaroslav Malina  Prof Michael J Hannon  Prof?Dr Viktor Brabec
Institution:1. Institute of Biophysics, Academy of Sciences of the Czech Republic, v.v.i. Kralovopolska 135, 612 65 Brno (Czech Republic);2. School of Chemistry, University of Birmingham, Edgbaston, Birmingham B15?2TT (UK)
Abstract:The dinuclear iron(II) supramolecular helicates Fe2L3]Cl4 (L=C25H20N4) bind to DNA through noncovalent (i.e., hydrogen‐bonding, electrostatic) interactions and exhibit antimicrobial and anticancer effects. In this study, we show that the helicates condense plasmid DNA with a much higher potency than conventional DNA‐condensing agents. Notably, molecules of DNA in the presence of the M enantiomer of Fe2L3]Cl4 do not form intermolecular aggregates typically formed by other condensing agents, such as spermidine or spermine. The helicates inhibit the activity of several DNA‐processing enzymes, such as RNA polymerase, DNA topoisomerase I, deoxyribonuclease I, and site‐specific restriction endonucleases. However, the results also indicate that the DNA condensation induced by the helicates does not play a crucial role in these inhibition reactions. The mechanisms for the inhibitory effects of Fe2L3]Cl4 helicates on DNA‐related enzymatic activities have been proposed.
Keywords:condensation  DNA  enzymes  helical structures  inhibition
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