Importance of Binding Affinity for the Activity of a Metallodendritic Chemical Nuclease.

A family of (2-pyridyl)amino-modified poly(amidoamine) dendrimer Cu complexes was prepared, and their chemical nuclease activities and binding affinity () levels for DNA plasmid were investigated. The values of the G2 to G6 apodendrimers for DNA plasmid were found to be 7.4, 23, 48, 70, and 280 µM, respectively, using ethidium bromide (EtBr) displacement experiments. The chemical nuclease activities of the corresponding complexes were determined by gel electrophoresis, and a clear positive dendritic effect was observed. Further analysis indicated a linear correlation between the values of the G2 to G5 apodendrimers and the nuclease activity of the corresponding complexes. This observation indicated the importance of substrate binding affinity for macromolecular nuclease activity. In addition, an experiment using 3'-(-hydroxyphenyl) fluorescein suggested that hydroxyl radicals formed under the tested conditions. Subsequently performed inhibition studies indicated that the hydroxyl radical was the active species responsible for the plasmid cleavage.