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Assessment of DNA-binding affinity of cholinesterase reactivators and electrophoretic determination of their effect on topoisomerase I and II activity
J. Janockova, E. Zilecka, J. Kasparkova, V. Brabec, O. Soukup, K. Kuca, M. Kozurkova,
Jazyk angličtina Země Anglie, Velká Británie
Typ dokumentu časopisecké články
PubMed
27412811
DOI
10.1039/c6mb00332j
Knihovny.cz E-zdroje
- MeSH
- cirkulární dichroismus MeSH
- denaturace nukleových kyselin MeSH
- DNA-topoisomerasy I chemie metabolismus MeSH
- DNA-topoisomerasy typu II chemie metabolismus MeSH
- DNA chemie metabolismus MeSH
- molekulární struktura MeSH
- reaktivátory cholinesterasy chemie farmakologie MeSH
- spektrální analýza MeSH
- vazba proteinů MeSH
- viskozita MeSH
- Publikační typ
- časopisecké články MeSH
In this paper, we describe the biochemical properties and biological activity of a series of cholinesterase reactivators (symmetrical bisquaternary xylene-linked compounds, K106-K114) with ctDNA. The interaction of the studied derivatives with ctDNA was investigated using UV-Vis, fluorescence, CD and LD spectrometry, and electrophoretic and viscometric methods. The binding constants K were estimated to be in the range 1.05 × 10(5)-5.14 × 10(6) M(-1) and the percentage of hypochromism was found to be 10.64-19.28% (from UV-Vis titration). The used methods indicate that the studied samples are groove binders. Electrophoretic methods proved that the studied compounds clearly influence calf thymus Topo I (at 5 μM concentration, except for compounds K107, K111 and K114 which were effective at higher concentrations) and human Topo II (K110 partially inhibited Topo II effects even at 5 μM concentration) activity.
Citace poskytuje Crossref.org
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