Assessment of DNA-binding affinity of cholinesterase reactivators and electrophoretic determination of their effect on topoisomerase I and II activity
Jazyk angličtina Země Anglie, Velká Británie Médium print
Typ dokumentu časopisecké články, práce podpořená grantem
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
- práce podpořená grantem MeSH
- Názvy látek
- DNA-topoisomerasy I MeSH
- DNA-topoisomerasy typu II MeSH
- DNA MeSH
- reaktivátory cholinesterasy 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.
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