caa a22 4500 605507058 CHVBK 20210128100630.0 cr unu---uuuuu 210128e20150901xx s 000 0 eng 10.1007/s00775-015-1282-2 doi (NATIONALLICENCE)springer-10.1007/s00775-015-1282-2 DNA binding and cleavage studies of copper(II) complexes with 2′-deoxyadenosine modified histidine moiety [Elektronische Daten] [Justyna Borowska, Malgorzata Sierant, Elzbieta Sochacka, Daniele Sanna, Elzbieta Lodyga-Chruscinska] This work is focused on the study of DNA binding and cleavage properties of 2′-deoxyadenosines modified with ester/amide of histidine (his6dA ester, his6dA amide) and their copper(II) complexes. To determine the coordination mode of the complex species potentiometric and spectroscopic (UV-visible, CD, EPR) studies have been performed. The analysis of electronic absorption and fluorescence spectra has been used to find the nature of the interactions between the compounds and calf thymus DNA (CT-DNA). There is significant influence of the -NH2 and -OCH3 groups on binding of the ligands or the complexes to DNA. Only amide derivative and its complex reveal intercalative ability. In the case of his6dA ester and Cu(II)-his6dA ester the main interactions can be groove binding. DNA cleavage activities of the compounds have been examined by gel electrophoresis. The copper complexes have promoted the cleavage of plasmid DNA, but none of the ligands exhibited any chemical nuclease activity. The application of different scavengers of reactive oxygen species provided a conclusion that DNA cleavage caused by copper complexes might occur via hydrolytic pathway. SBIC, 2015 Artificial nucleases nationallicence Copper complexes nationallicence Histidine derivatives nationallicence Borowska Justyna Institute of General Food Chemistry, Lodz University of Technology, ul. Stefanowskiego 4/10, 90-924, Lodz, Poland aut Sierant Malgorzata Centre of Molecular and Macromolecular Studies, Polish Academy of Science, ul. Sienkiewicza 112, 90-363, Lodz, Poland aut Sochacka Elzbieta Institute of Organic Chemistry, Lodz University of Technology, ul. Zeromskiego 176, 90-924, Lodz, Poland aut Sanna Daniele Istituto C.N.R. Chimica Biomolecolare, Trav. La Crucca 3, reg. Baldinca, 07040, Sassari, Italy aut Lodyga-Chruscinska Elzbieta Institute of General Food Chemistry, Lodz University of Technology, ul. Stefanowskiego 4/10, 90-924, Lodz, Poland aut JBIC Journal of Biological Inorganic Chemistry Springer Berlin Heidelberg 20/6(2015-09-01), 989-1004 0949-8257 20:6<989 2015 20 775 https://doi.org/10.1007/s00775-015-1282-2 text/html Onlinezugriff via DOI BK010053 XK010053 XK010000 Metadata rights reserved Springer special CC-BY-NC licence nationallicence 1 research-article jats NATIONALLICENCE NATIONALLICENCE NL-springer NATIONALLICENCE 856 40 https://doi.org/10.1007/s00775-015-1282-2 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Borowska Justyna Institute of General Food Chemistry, Lodz University of Technology, ul. Stefanowskiego 4/10, 90-924, Lodz, Poland aut NATIONALLICENCE 700 1- Sierant Malgorzata Centre of Molecular and Macromolecular Studies, Polish Academy of Science, ul. Sienkiewicza 112, 90-363, Lodz, Poland aut NATIONALLICENCE 700 1- Sochacka Elzbieta Institute of Organic Chemistry, Lodz University of Technology, ul. Zeromskiego 176, 90-924, Lodz, Poland aut NATIONALLICENCE 700 1- Sanna Daniele Istituto C.N.R. Chimica Biomolecolare, Trav. La Crucca 3, reg. Baldinca, 07040, Sassari, Italy aut NATIONALLICENCE 700 1- Lodyga-Chruscinska Elzbieta Institute of General Food Chemistry, Lodz University of Technology, ul. Stefanowskiego 4/10, 90-924, Lodz, Poland aut NATIONALLICENCE 773 0- JBIC Journal of Biological Inorganic Chemistry Springer Berlin Heidelberg 20/6(2015-09-01), 989-1004 0949-8257 20:6<989 2015 20 775