Assessment of DNA-binding affinity of cholinesterase reactivators and electrophoretic determination of their effect on topoisomerase I and II activity
Language English Country England, Great Britain Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
27412811
DOI
10.1039/c6mb00332j
Knihovny.cz E-resources
- MeSH
- Circular Dichroism MeSH
- Nucleic Acid Denaturation MeSH
- DNA Topoisomerases, Type I chemistry metabolism MeSH
- DNA Topoisomerases, Type II chemistry metabolism MeSH
- DNA chemistry metabolism MeSH
- Molecular Structure MeSH
- Cholinesterase Reactivators chemistry pharmacology MeSH
- Spectrum Analysis MeSH
- Protein Binding MeSH
- Viscosity MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- DNA Topoisomerases, Type I MeSH
- DNA Topoisomerases, Type II MeSH
- DNA MeSH
- Cholinesterase Reactivators 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.
References provided by Crossref.org
